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enzyme (lysozyme)

 
Enzymes
  Enzyme classes:
  EC 1: Oxidoreductases
  EC 2: Transferases
    EC 2.1
    EC 2.2
    EC 2.3
    EC 2.4
    EC 2.5
    EC 2.6
      EC 2.6.1
        EC 2.6.1.1
        EC 2.6.1.2
        EC 2.6.1.3
        EC 2.6.1.4
        EC 2.6.1.5
        EC 2.6.1.6
        EC 2.6.1.7
        EC 2.6.1.8
        EC 2.6.1.9
        EC 2.6.1.10
        EC 2.6.1.11
        EC 2.6.1.12
        EC 2.6.1.13
        EC 2.6.1.14
        EC 2.6.1.15
        EC 2.6.1.16
        EC 2.6.1.17
        EC 2.6.1.18
        EC 2.6.1.19
        EC 2.6.1.20
        EC 2.6.1.21
        EC 2.6.1.22
        EC 2.6.1.23
        EC 2.6.1.24
        EC 2.6.1.25
        EC 2.6.1.26
        EC 2.6.1.27
        EC 2.6.1.28
        EC 2.6.1.29
        EC 2.6.1.30
        EC 2.6.1.31
        EC 2.6.1.32
        EC 2.6.1.33
        EC 2.6.1.34
        EC 2.6.1.35
        EC 2.6.1.36
        EC 2.6.1.37
        EC 2.6.1.38
        EC 2.6.1.39
        EC 2.6.1.40
        EC 2.6.1.41
        EC 2.6.1.42
        EC 2.6.1.43
        EC 2.6.1.44
        EC 2.6.1.45
        EC 2.6.1.46
        EC 2.6.1.47
        EC 2.6.1.48
        EC 2.6.1.49
        EC 2.6.1.50
        EC 2.6.1.51
        EC 2.6.1.52
        EC 2.6.1.53
        EC 2.6.1.54
        EC 2.6.1.55
        EC 2.6.1.56
        EC 2.6.1.57
        EC 2.6.1.58
        EC 2.6.1.59
        EC 2.6.1.60
        EC 2.6.1.61
        EC 2.6.1.62
        EC 2.6.1.63
        EC 2.6.1.64
        EC 2.6.1.65
        EC 2.6.1.66
        EC 2.6.1.67
        EC 2.6.1.68
        EC 2.6.1.69
        EC 2.6.1.70
        EC 2.6.1.71
        EC 2.6.1.72
        EC 2.6.1.73
        EC 2.6.1.74
        EC 2.6.1.75
        EC 2.6.1.76
        EC 2.6.1.77
        EC 2.6.1.78
        EC 2.6.1.79
        EC 2.6.1.80
        EC 2.6.1.81
        EC 2.6.1.82
        EC 2.6.1.83
        EC 2.6.1.84
        EC 2.6.1.85
        EC 2.6.1.86
      EC 2.6.2
      EC 2.6.3
      EC 2.6.99
    EC 2.7
    EC 2.8
    EC 2.9
  EC 3: Hydrolases
  EC 4: Lyases
  EC 5: Isomerases
  EC 6: Ligases
  General information:
  Catalytic mechanism
  Enzyme kinetics
  Inhibitors
  Enzymes in industry

EC 2.6.1.1 - L- aspartate:2- oxoglutarate aminotransferase (aspartate transaminase)



3D structures of EC 2.6.1.1 - aspartate transaminase in Protein Data Bank

updated: 6 January 2022, 2:15

In total: 163 PDB structures of EC 2.6.1.1 - aspartate transaminase:
  1. 1aam: The Structural Basis for The Altered Substrate Specificity of The R292D Active Site Mutant of Aspartate Aminotransferase from E. Coli
  2. 1aat: Oxoglutarate-induced Conformational Changes in Cytosolic Aspartate Aminotransferase
  3. 1aaw: The Structural Basis for The Altered Substrate Specificity of The R292D Active Site Mutant of Aspartate Aminotransferase from E. Coli
  4. 1ahe: Aspartate Aminotransferase Hexamutant
  5. 1ahf: Aspartate Aminotransferase Hexamutant
  6. 1ahg: Aspartate Aminotransferase Hexamutant
  7. 1ahx: Aspartate Aminotransferase Hexamutant
  8. 1ahy: Aspartate Aminotransferase Hexamutant
  9. 1aia: Structural Basis for The Catalytic Activity of Aspartate Aminotransferase K258H Lacking The Pyridoxal-5'-phosphate Binding Lysine Residue
  10. 1aib: Structural Basis for The Catalytic Activity of Aspartate Aminotransferase K258H Lacking The Pyridoxal-5'-phsophate Binding Lysine Residue
  11. 1aic: Structural Basis for The Catalytic Activity of Aspartate Aminotransferase K258H Lacking The Pyridoxal-5'-phsophate Binding Lysine Residue
  12. 1ajr: Refinement and Comparison of The Crystal Structures of Pig Cytosolic Aspartate Aminotransferase and Its Complex with 2-methylaspartate
  13. 1ajs: Refinement and Comparison of The Crystal Structures of Pig Cytosolic Aspartate Aminotransferase and Its Complex with 2-methylaspartate
  14. 1aka: Structural Basis for The Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-phosphate- Binding Lysine Residue
  15. 1akb: Structural Basis for The Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-phosphate- Binding Lysine Residue
  16. 1akc: Structural Basis for The Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-phosphate- Binding Lysine Residue
  17. 1ama: Domain Closure in Mitochondrial Aspartate Aminotransferase
  18. 1amq: X-ray Crystallographic Study of Pyridoxamine 5'-phosphate- Type Aspartate Aminotransferases from Escherichia Coli in Three Forms
  19. 1amr: X-ray Crystallographic Study of Pyridoxamine 5'-phosphate- Type Aspartate Aminotransferases from Escherichia Coli in Three Forms
  20. 1ams: X-ray Crystallographic Study of Pyridoxamine 5'-phosphate- Type Aspartate Aminotransferases from Escherichia Coli in Three Forms
  21. 1arg: Aspartate Aminotransferase, Phospho-5'-pyridoxyl Aspartate Complex
  22. 1arh: Aspartate Aminotransferase, Y225R/R386A Mutant
  23. 1ari: Aspartate Aminotransferase, W140H Mutant, Maleate Complex
  24. 1ars: X-ray Crystallographic Study of Pyridoxal 5'-phosphate-type Aspartate Aminotransferases from Escherichia Coli in Open and Closed Form
  25. 1art: X-ray Crystallographic Study of Pyridoxal 5'-phosphate-type Aspartate Aminotransferases from Escherichia Coli in Open and Closed Form
  26. 1asa: The Structural Basis for The Reduced Activity of The Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
  27. 1asb: The Structural Basis for The Reduced Activity of The D223A(D222A) Active Site Mutant of E. Coli Aspartate Aminotransferase
  28. 1asc: The Structural Basis for The Reduced Activity of The D223A(D222A) Active Site Mutant of E. Coli Aspartate Aminotransferase
  29. 1asd: The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with N-meplp
  30. 1ase: The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with Plp-n-oxide
  31. 1asf: The Structural Basis for The Reduced Activity of The Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
  32. 1asg: The Structural Basis for The Reduced Activity of The Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
  33. 1asl: Crystal Structures of Escherichia Coli Aspartate Aminotransferase in Two Conformations: Comparison of an Unliganded Open and Two Liganded Closed Forms
  34. 1asm: Crystal Structures of Escherichia Coli Aspartate Aminotransferase in Two Conformations: Comparison of an Unliganded Open and Two Liganded Closed Forms
  35. 1asn: Crystal Structures of Escherichia Coli Aspartate Aminotransferase in Two Conformations: Comparison of an Unliganded Open and Two Liganded Closed Forms
  36. 1b4x: Aspartate Aminotransferase from E. Coli, C191S Mutation, with Bound Maleate
  37. 1b5o: Thermus Thermophilus Aspartate Aminotransferase Single Mutant 1
  38. 1b5p: Thermus Thermophilus Aspartate Aminotransferase Double Mutant 1
  39. 1bjw: Aspartate Aminotransferase from Thermus Thermophilus
  40. 1bkg: Aspartate Aminotransferase from Thermus Thermophilus with Maleate
  41. 1bqa: Aspartate Aminotransferase P195A Mutant
  42. 1bqd: Aspartate Aminotransferase P138A/P195A Double Mutant
  43. 1c9c: Aspartate Aminotransferase Complexed with C3-pyridoxal-5'- Phosphate
  44. 1cq6: Aspartate Aminotransferase Complex with C4-pyridoxal-5p- Phosphate
  45. 1cq7: Aspartate Aminotransferase (e.c. 2.6.1.1) Complexed with C5- Pyridoxal-5p-phosphate
  46. 1cq8: Aspartate Aminotransferase (e.c. 2.6.1.1) Complexed with C6- Pyridoxal-5p-phosphate
  47. 1czc: Aspartate Aminotransferase Mutant Atb17/139s/142n with Glutaric Acid
  48. 1cze: Aspartate Aminotransferase Mutant Atb17/139s/142n with Succinic Acid
  49. 1g4v: Aspartate Aminotransferase Active Site Mutant N194A/Y225F
  50. 1g4x: Aspartate Aminotransferase Active Site Mutant N194A/R292L
  51. 1g7w: Aspartate Aminotransferase Active Site Mutant N194A/R386L
  52. 1g7x: Aspartate Aminotransferase Active Site Mutant N194A/R292L/R386L
  53. 1gc3: Thermus Thermophilus Aspartate Aminotransferase Tetra Mutant 2 Complexed with Tryptophan
  54. 1gc4: Thermus Thermophilus Aspartate Aminotransferase Tetra Mutant 2 Complexed with Aspartate
  55. 1gck: Thermus Thermophilus Aspartate Aminotransferase Double Mutant 1 Complexed with Aspartate
  56. 1ivr: Structure of Aspartate Aminotransferase
  57. 1ix6: Aspartate Aminotransferase Active Site Mutant V39F
  58. 1ix7: Aspartate Aminotransferase Active Site Mutant V39F Maleate Complex
  59. 1ix8: Aspartate Aminotransferase Active Site Mutant V39F/N194A
  60. 1j32: Aspartate Aminotransferase from Phormidium Lapideum
  61. 9aat: X-ray Structure Refinement and Comparison of Three Forms of Mitochondrial Aspartate Aminotransferase
  62. 8aat: X-ray Structure Refinement and Comparison of Three Forms of Mitochondrial Aspartate Aminotransferase
  63. 7aat: X-ray Structure Refinement and Comparison of Three Forms of Mitochondrial Aspartate Aminotransferase
  64. 5eaa: Aspartate Aminotransferase from E. Coli, C191S Mutation
  65. 5bj4: Thermus Thermophilus Aspartate Aminotransferase Tetra Mutant 2
  66. 5bj3: Thermus Thermophilus Aspartate Aminotransferase Tetra Mutant 1
  67. 3pdb: Crystal Structure of Mouse Mitochondrial Aspartate Aminotransferase in Complex with Oxaloacetic Acid
  68. 3pd6: Crystal Structure of Mouse Mitochondrial Aspartate Aminotransferase, a Newly Identified Kynurenine Aminotransferase-iv
  69. 3paa: Mechanism of Inactivation of E. Coli Aspartate Aminotransferase by (s)-4-amino-4,5-dihydro-2-furancarboxylic Acid (s-adfa) Ph 8.0
  70. 3pa9: Mechanism of Inactivation of E. Coli Aspartate Aminotransferase by (s)-4-amino-4,5-dihydro-2-furancarboxylic Acid (s-adfa) Ph 7.5
  71. 1map: Crystal Structures of True Enzymatic Reaction Intermediates: Aspartate and Glutamate Ketimines in Aspartate Aminotransferase
  72. 1maq: Crystal Structures of True Enzymatic Reaction Intermediates: Aspartate and Glutamate Ketimines in Aspartate Aminotransferase
  73. 3meb: Structure of Cytoplasmic Aspartate Aminotransferase from Giardia Lamblia
  74. 1o4s: Crystal Structure of Aspartate Aminotransferase (tm1255) from Thermotoga Maritima at 1.90 a Resolution
  75. 3k7y: Aspartate Aminotransferase of Plasmodium Falciparum
  76. 1oxo: Aspartate Aminotransferase, H-asp Complex, Open Conformation
  77. 1oxp: Aspartate Aminotransferase, H-asp Complex, Closed Conformation
  78. 3ii0: Crystal Structure of Human Glutamate Oxaloacetate Transaminase 1 (got1)
  79. 1qir: Aspartate Aminotransferase from Escherichia Coli, C191Y Mutation, with Bound Maleate
  80. 1qis: Aspartate Aminotransferase from Escherichia Coli, C191F Mutation, with Bound Maleate
  81. 1qit: Aspartate Aminotransferase from Escherichia Coli, C191W Mutation, with Bound Maleate
  82. 3hlm: Crystal Structure of Mouse Mitochondrial Aspartate Aminotransferase/kynurenine Aminotransferase IV
  83. 1spa: Role of Asp222 in The Catalytic Mechanism of Escherichia Coli Aspartate Aminotransferase: The Amino Acid Residue Which Enhances The Function of The Enzyme-bound Coenzyme Pyridoxal 5'-phosphate
  84. 3f6t: Crystal Structure of Aspartate Aminotransferase (e.c. 2.6.1.1) (yp_194538.1) from Lactobacillus Acidophilus Ncfm at 2.15 a Resolution
  85. 1tar: Crystalline Mitochondrial Aspartate Aminotransferase Exists in Only Two Conformations
  86. 1tas: Crystalline Mitochondrial Aspartate Aminotransferase Exists in Only Two Conformations
  87. 1tat: Crystalline Mitochondrial Aspartate Aminotransferase Exists in Only Two Conformations
  88. 1toe: Unliganded Structure of Hexamutant + A293D Mutant of E. Coli Aspartate Aminotransferase
  89. 1tog: Hydrocinnamic Acid-bound Structure of Srhept + A293D Mutant of E. Coli Aspartate Aminotransferase
  90. 1toi: Hydrocinnamic Acid-bound Structure of Hexamutant + A293D Mutant of E. Coli Aspartate Aminotransferase
  91. 1toj: Hydrocinnamic Acid-bound Structure of Srhept Mutant of E. Coli Aspartate Aminotransferase
  92. 1tok: Maleic Acid-bound Structure of Srhept Mutant of E. Coli Aspartate Aminotransferase
  93. 3aat: Activity and Structure of The Active-site Mutants R386Y and R386F of Escherichia Coli Aspartate Aminotransferase
  94. 1x28: Crystal Structure of E.coli Aspat Complexed with N- Phosphopyridoxyl-l-glutamic Acid
  95. 1x29: Crystal Structure of E.coli Aspat Complexed with N- Phosphopyridoxyl-2-methyl-l-glutamic Acid
  96. 1x2a: Crystal Structure of E.coli Aspat Complexed with N- Phosphopyridoxyl-d-glutamic Acid
  97. 2z61: Crystal Structure of Mj0684 from Methanococcus Jannaschii Reveals Its Similarity in The Active Site to Kynurenine Aminotransferases
  98. 1yaa: Aspartate Aminotransferase from Saccharomyces Cerevisiae Cytoplasm
  99. 1yoo: Aspartate Aminotransferase Mutant Atb17 with Isovaleric Acid
  100. 6lig: Crystal Structure of Human Glutamate Oxaloacetate Transaminase 1 (got1) in Complex with Ah
  101. 2aat: 2.8-angstroms-resolution Crystal Structure of an Active- Site Mutant of Aspartate Aminotransferase from Escherichia Coli
  102. 2qbt: Structural Studies Reveal The Inactivation of E. Coli L- Aspartate Aminotransferase by (s)-4,5-amino-dihydro-2- Thiophenecarboxylic Acid (sadta) via Two Mechanisms (at Ph 8.0)
  103. 2qb3: Structural Studies Reveal The Inactivation of E. Coli L- Aspartate Aminotransferase by (s)-4,5-dihydro-2- Thiophenecarboxylic Acid (sadta) via Two Mechanisms (at Ph 7.5)
  104. 2qb2: Structural Studies Reveal The Inactivation of E. Coli L- Aspartate Aminotransferase by (s)-4,5-dihydro- 2thiophenecarboylic Acid (sadta) via Two Mechanisms (at Ph 7.0).
  105. 2qa3: Structural Studies Reveal The Inactivation of E. Coli L- Aspartate Aminotransferase by (s)-4,5-amino-dihydro-2- Thiophenecarboxylic Acid (sadta) via Two Mechanisms (at Ph6.5)
  106. 2q7w: Structural Studies Reveals The Inactivation of E. Coli L- Aspartate Aminotransferase (s)-4,5-amino-dihydro-2- Thiophenecarboxylic Acid (sadta) via Two Mechanisms at Ph 6.0
  107. 2cst: Crystal Structure of The Closed Form of Chicken Cytosolic Aspartate Aminotransferase at 1.9 Angstroms Resolution
  108. 2d5y: Aspartate Aminotransferase Mutant Mc with Isovaleric Acid
  109. 2d61: Aspartate Aminotransferase Mutant Ma with Maleic Acid
  110. 2d63: Aspartate Aminotransferase Mutant Ma with Isovaleric Acid
  111. 2d64: Aspartate Aminotransferase Mutant Mabc with Isovaleric Acid
  112. 2d65: Aspartate Aminotransferase Mutant Mabc
  113. 2d66: Aspartate Aminotransferase Mutant Mab
  114. 2d7y: Aspartate Aminotransferase Mutant Ma
  115. 2d7z: Aspartate Aminotransferase Mutant Mab Complexed with Maleic Acid
  116. 2o1b: Structure of Aminotransferase from Staphylococcus Aureus
  117. 3ppl: Crystal Structure of an Aspartate Transaminase (ncgl0237, Cgl0240) from Corynebacterium Glutamicum Atcc 13032 Kitasato at 1.25 a Resolution
  118. 3qn6: Crystal Structures of Escherichia Coli Aspartate Aminotransferase Reconstituted with 1-deaza-pyridoxal 5'-phosphate: Internal Aldimine and Stable L-aspartate External Aldimine
  119. 3qpg: Crystal Structures of Escherichia Coli Aspartate Aminotransferase Reconstituted with 1-deaza-pyridoxal 5'-phosphate: Internal Aldimine and Stable L-aspartate External Aldimine
  120. 3zzj: Structure of an Engineered Aspartate Aminotransferase
  121. 3zzk: Structure of an Engineered Aspartate Aminotransferase
  122. 4a00: Structure of an Engineered Aspartate Aminotransferase
  123. 4eu1: Structure of a Mitochondrial Aspartate Aminotransferase from Trypanosoma Brucei
  124. 6jpk: Crystal Structure of S. Pombe Aspartate Aminotransferase
  125. 4h51: Crystal Structure of a Putative Aspartate Aminotransferase from Leishmania Major Friedlin
  126. 4dbc: Substrate Activation in Aspartate Aminotransferase
  127. 4f5f: Structure of Aspartate Aminotransferase Conversion to Tyrosine Aminotransferase: Chimera P1.
  128. 4f5g: Rational Design and Directed Evolution of E. Coli Apartate Aminotransferase to Tyrosine Aminotransferase: Mutant P2.
  129. 4f5h: Intercoversion of Substrate Specificity: E. Coli Aspatate Aminotransferase to Tyrosine Aminotransferase: Chimera P3.
  130. 4f5i: Substrate Specificity Conversion of E. Coli Pyridoxal-5'-phosphate Dependent Aspartate Aminotransferase to Tyrosine Aminotransferase: Chimera P4.
  131. 4f5j: Rational Design and Directed Evolution for Conversion of Substrate Specificity from E.coli Aspartate Aminotransferase to Tyrosine Aminotransferase: Mutant P5.
  132. 4f5k: Substrate Specificity Conversion of Aspartate Aminotransferase to Tyrosine Aminotransferase by The Janus Algorithm: Chimera P6.
  133. 4f5m: Wild-type E. Coli Aspartate Aminotransferase: a Template for The Interconversion of Substrate Specificity and Activity to Tyrosine Aminotransferase by The Janus Algorithm.
  134. 4f5l: A Theoretical Optimized Mutant for The Conversion of Substrate Specificity and Activity of Aspartate Aminotransferase to Tyrosine Aminotransferase: Chimera P7.
  135. 6f77: Crystal Structure of The Prephenate Aminotransferase from Rhizobium Meliloti
  136. 6f5v: Crystal Structure of The Prephenate Aminotransferase from Arabidopsis Thaliana
  137. 6f35: Crystal Structure of The Aspartate Aminotranferase from Rhizobium Meliloti
  138. 6ezl: Crystal Structure of Aspartate Aminotransferase from Trypanosoma Cruzi at 2.07 Angstrom Resolution
  139. 6dnd: Crystal Structure of Wild-type (wt) Human Glutamate Oxaloacetate Transaminase 1 (got1)
  140. 6dnb: Crystal Structure of T110A:S256A Mutant Human Glutamate Oxaloacetate Transaminase 1 (got1)
  141. 6dna: Crystal Structure of T110A Mutant Human Glutamate Oxaloacetate Transaminase 1 (got1)
  142. 5wml: Arabidopsis Thaliana Prephenate Aminotransferase Mutant- K306A
  143. 5wmk: Arabidopsis Thaliana Prephenate Aminotransferase Double Mutant- T84V K169V
  144. 5wmi: Arabidopsis Thaliana Prephenate Aminotransferase Mutant- T84V
  145. 5wmh: Arabidopsis Thaliana Prephenate Aminotransferase
  146. 5vwr: E.coli Aspartate Aminotransferase-(1r,3s,4s)-3-amino-4- Fluorocyclopentane-1-carboxylic Acid (fcp)-alpha-ketoglutarate
  147. 5vwq: E.coli Aspartate Aminotransferase-(1r,3s,4s)-3-amino-4- Fluorocyclopentane-1-carboxylic Acid (fcp)
  148. 5vk7: Aspartate Aminotransferase Ph 4.0
  149. 5vjz: Joint X-ray/neutron Structure of Aspartate Aminotransferase with Alpha-methyl-aspartate at Ph 7.5
  150. 4w5k: Structure of a Mitochondrial Aspartate Aminotransferase from Trypanosoma Brucei, K237A Mutant
  151. 5tot: Crystal Structure of Aat H143L:H189L Double Mutant
  152. 5tor: Crystal Structure of Aat D222T Mutant
  153. 5toq: High Resolution Crystal Structure of Aat
  154. 5ton: Crystal Structure of Aat H143L Mutant
  155. 5t4l: Plp and Gaba Trigger Gabr-mediated Transcription Regulation in Bacillus Subsidies via External Aldimine Formation
  156. 5iwq: Crystal Structure of Aspartate Aminotransferase (aspat) from Corynebacterium Glutamicum Atcc 13032
  157. 5hxx: Crystal Structure of Aspat from Corynebacterium Glutamicum
  158. 5ax8: Recombinant Expression, Purification and Preliminary Crystallographic Studies of The Mature Form of Human Mitochondrial Aspartate Aminotransferase
  159. 3wzf: Crystal Structure of Human Cytoplasmic Aspartate Aminotransferase
  160. 7kz3: Crystal Structure of Kaba from Bacillus Cereus Uw85 in Complex with The Internal Aldimine
  161. 7kz5: Crystal Structure of Kaba from Bacillus Cereus Uw85 in Complex with The Plp External Aldimine Adduct with Kanosamine-6-phosphate
  162. 7kz6: Crystal Structure of Kaba from Bacillus Cereus Uw85 with Bound Cofactor Pmp
  163. 7kzd: Crystal Structure of Kaba from Bacillus Cereus Uw85 in Complex with The Reduced Internal Aldimine and with Bound Glutarate
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