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enzyme (lysozyme)

 
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  EC 1: Oxidoreductases
  EC 2: Transferases
  EC 3: Hydrolases
    EC 3.1
    EC 3.2
    EC 3.3
    EC 3.4
      EC 3.4.1
      EC 3.4.2
      EC 3.4.3
      EC 3.4.4
      EC 3.4.11
      EC 3.4.12
      EC 3.4.13
      EC 3.4.14
      EC 3.4.15
      EC 3.4.16
      EC 3.4.17
      EC 3.4.18
      EC 3.4.19
      EC 3.4.21
        EC 3.4.21.1
        EC 3.4.21.2
        EC 3.4.21.3
        EC 3.4.21.4
        EC 3.4.21.5
        EC 3.4.21.6
        EC 3.4.21.7
        EC 3.4.21.8
        EC 3.4.21.9
        EC 3.4.21.10
        EC 3.4.21.11
        EC 3.4.21.12
        EC 3.4.21.13
        EC 3.4.21.14
        EC 3.4.21.15
        EC 3.4.21.16
        EC 3.4.21.17
        EC 3.4.21.18
        EC 3.4.21.19
        EC 3.4.21.20
        EC 3.4.21.21
        EC 3.4.21.22
        EC 3.4.21.23
        EC 3.4.21.24
        EC 3.4.21.25
        EC 3.4.21.26
        EC 3.4.21.27
        EC 3.4.21.28
        EC 3.4.21.29
        EC 3.4.21.30
        EC 3.4.21.31
        EC 3.4.21.32
        EC 3.4.21.33
        EC 3.4.21.34
        EC 3.4.21.35
        EC 3.4.21.36
        EC 3.4.21.37
        EC 3.4.21.38
        EC 3.4.21.39
        EC 3.4.21.40
        EC 3.4.21.41
        EC 3.4.21.42
        EC 3.4.21.43
        EC 3.4.21.44
        EC 3.4.21.45
        EC 3.4.21.46
        EC 3.4.21.47
        EC 3.4.21.48
        EC 3.4.21.49
        EC 3.4.21.50
        EC 3.4.21.51
        EC 3.4.21.52
        EC 3.4.21.53
        EC 3.4.21.54
        EC 3.4.21.55
        EC 3.4.21.56
        EC 3.4.21.57
        EC 3.4.21.58
        EC 3.4.21.59
        EC 3.4.21.60
        EC 3.4.21.61
        EC 3.4.21.62
        EC 3.4.21.63
        EC 3.4.21.64
        EC 3.4.21.65
        EC 3.4.21.66
        EC 3.4.21.67
        EC 3.4.21.68
        EC 3.4.21.69
        EC 3.4.21.70
        EC 3.4.21.71
        EC 3.4.21.72
        EC 3.4.21.73
        EC 3.4.21.74
        EC 3.4.21.75
        EC 3.4.21.76
        EC 3.4.21.77
        EC 3.4.21.78
        EC 3.4.21.79
        EC 3.4.21.80
        EC 3.4.21.81
        EC 3.4.21.82
        EC 3.4.21.83
        EC 3.4.21.84
        EC 3.4.21.85
        EC 3.4.21.86
        EC 3.4.21.87
        EC 3.4.21.88
        EC 3.4.21.89
        EC 3.4.21.90
        EC 3.4.21.91
        EC 3.4.21.92
        EC 3.4.21.93
        EC 3.4.21.94
        EC 3.4.21.95
        EC 3.4.21.96
        EC 3.4.21.97
        EC 3.4.21.98
        EC 3.4.21.99
        EC 3.4.21.100
        EC 3.4.21.101
        EC 3.4.21.102
        EC 3.4.21.103
        EC 3.4.21.104
        EC 3.4.21.105
        EC 3.4.21.106
        EC 3.4.21.107
        EC 3.4.21.108
        EC 3.4.21.109
        EC 3.4.21.110
        EC 3.4.21.111
        EC 3.4.21.112
        EC 3.4.21.113
        EC 3.4.21.114
        EC 3.4.21.115
        EC 3.4.21.116
        EC 3.4.21.117
        EC 3.4.21.118
        EC 3.4.21.119
        EC 3.4.21.120
      EC 3.4.22
      EC 3.4.23
      EC 3.4.24
      EC 3.4.25
      EC 3.4.99
    EC 3.5
    EC 3.6
    EC 3.7
    EC 3.8
    EC 3.9
    EC 3.10
    EC 3.11
    EC 3.12
    EC 3.13
  EC 4: Lyases
  EC 5: Isomerases
  EC 6: Ligases
  General information:
  Catalytic mechanism
  Enzyme kinetics
  Inhibitors
  Enzymes in industry

EC 3.4.21.12 - α- Lytic endopeptidase (\xCE\xB1- lytic endopeptidase)



3D structures of EC 3.4.21.12 - \xCE\xB1-lytic endopeptidase in Protein Data Bank

updated: 6 January 2022, 2:15

In total: 46 PDB structures of EC 3.4.21.12 - \xCE\xB1-lytic endopeptidase:
  1. 1boq: Pro Region C-terminus: Protease Active Site Interactions Are Critical in Catalyzing The Folding of Alpha-lytic Protease
  2. 1gba: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Ala
  3. 1gbb: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Ala Complex with Methoxysuccinyl-ala-ala- Pro-alanine Boronic Acid
  4. 1gbc: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Ala Complex with Methoxysuccinyl-ala-ala- Pro-leucine Boronic Acid
  5. 1gbd: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Ala Complex with Methoxysuccinyl-ala-ala- Pro-phenylalanine Boronic Acid
  6. 1gbe: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Leu
  7. 1gbf: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Leu Complex with Methoxysuccinyl-ala-ala- Pro-alanine Boronic Acid
  8. 1gbh: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Leu Complex with Methoxysuccinyl-ala-ala- Pro-leucine Boronic Acid
  9. 1gbi: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Leu Complex with Methoxysuccinyl-ala-ala- Pro-phenylalanine Boronic Acid
  10. 1gbj: Alpha-lytic Protease with Met 190 Replaced by Ala
  11. 1gbk: Alpha-lytic Protease with Met 190 Replaced by Ala Complex with Methoxysuccinyl-ala-ala-pro-alanine Boronic Acid
  12. 1gbl: Alpha-lytic Protease with Met 190 Replaced by Ala Complex with Methoxysuccinyl-ala-ala-pro-leucine Boronic Acid
  13. 1gbm: Alpha-lytic Protease with Met 190 Replaced by Ala Complex with Methoxysuccinyl-ala-ala-pro-phenylalanine Boronic Acid
  14. 9lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
  15. 8lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
  16. 7lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
  17. 6lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
  18. 5lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
  19. 3lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
  20. 1p01: Serine Protease Mechanism. Structure of an Inhibitory Complex of Alpha-lytic Protease and a Tightly Bound Peptide Boronic Acid
  21. 1p02: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
  22. 1p03: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
  23. 1p04: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
  24. 1p05: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
  25. 1p06: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
  26. 1p09: Structural Plasticity as a Determinant of Enzyme Specificity. Creating Broadly Specific Proteases
  27. 1p10: Structural Plasticity as a Determinant of Enzyme Specificity. Creating Broadly Specific Proteases
  28. 1p11: Crystal Structures of Alpha-lytic Protease Complexes with Irreversibly Bound Phosphonate Esters
  29. 1p12: Crystal Structures of Alpha-lytic Protease Complexes with Irreversibly Bound Phosphonate Esters
  30. 1qq4: Crystal Structure of an Alpha-lytic Protease Mutant with Accelerated Folding Kinetics, R102H/G134S
  31. 1qrw: Crystal Structure of an Alpha-lytic Protease Mutant with Accelerated Folding Kinetics, R102H/G134S, Ph 8
  32. 1qrx: Crystal Structure of Wild-type Alpha-lytic Protease at 1.6 A, Ph 5.14
  33. 1ssx: 0.83a Resolution Crystal Structure of Alpha-lytic Protease at Ph 8
  34. 1tal: Alpha-lytic Protease at 120 K (single Structure Model)
  35. 2alp: Refined Structure of Alpha-lytic Protease at 1.7 Angstroms Resolution. Analysis of Hydrogen Bonding and Solvent Structure
  36. 2ull: Multiple Conformation Structure of Alpha-lytic Protease at 120 K
  37. 2lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
  38. 2h5c: 0.82a Resolution Crystal Structure of Alpha-lytic Protease at Ph 5
  39. 2h5d: 0.9a Resolution Crystal Structure of Alpha-lytic Protease Complexed with a Transition State Analogue, Meosuc-ala-ala- Pro-val Boronic Acid
  40. 3m7t: Crystal Structure of Alpha-lytic Protease Sb2+3 E8A/R105S Mutant
  41. 3m7u: Crystal Structure of Alpha-lytic Protease Sb1+2 R64A/E182Q Mutant
  42. 3qgj: 1.3a Structure of Alpha-lytic Protease Bound to Ac-alaalapro-alanal
  43. 3urc: T181G Mutant of Alpha-lytic Protease
  44. 3urd: T181A Mutant of Alpha-lytic Protease
  45. 3ure: Repack Mutant (T181I, W199L, Q210I) of Alpha-lytic Protease
  46. 5wot: Nmr Solution Structure of A-lytic Protease Using Two 4d-spectra
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