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Enzymes
  Enzyme classes:
  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:

1boq: Pro Region C-terminus: Protease Active Site Interactions Are Critical in Catalyzing The Folding of Alpha-lytic Protease
1gba: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Ala
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
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
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
1gbe: Alpha-lytic Protease with Met 190 Replaced by Ala and Gly 216 Replaced by Leu
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
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
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
1gbj: Alpha-lytic Protease with Met 190 Replaced by Ala
1gbk: Alpha-lytic Protease with Met 190 Replaced by Ala Complex with Methoxysuccinyl-ala-ala-pro-alanine Boronic Acid
1gbl: Alpha-lytic Protease with Met 190 Replaced by Ala Complex with Methoxysuccinyl-ala-ala-pro-leucine Boronic Acid
1gbm: Alpha-lytic Protease with Met 190 Replaced by Ala Complex with Methoxysuccinyl-ala-ala-pro-phenylalanine Boronic Acid
9lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
8lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
7lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
6lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
5lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
3lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
1p01: Serine Protease Mechanism. Structure of an Inhibitory Complex of Alpha-lytic Protease and a Tightly Bound Peptide Boronic Acid
1p02: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
1p03: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
1p04: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
1p05: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
1p06: Structure Analysis of Specificity. Alpha-lytic Protease Complexes with Analogues of Reaction Intermediates
1p09: Structural Plasticity as a Determinant of Enzyme Specificity. Creating Broadly Specific Proteases
1p10: Structural Plasticity as a Determinant of Enzyme Specificity. Creating Broadly Specific Proteases
1p11: Crystal Structures of Alpha-lytic Protease Complexes with Irreversibly Bound Phosphonate Esters
1p12: Crystal Structures of Alpha-lytic Protease Complexes with Irreversibly Bound Phosphonate Esters
1qq4: Crystal Structure of an Alpha-lytic Protease Mutant with Accelerated Folding Kinetics, R102H/G134S
1qrw: Crystal Structure of an Alpha-lytic Protease Mutant with Accelerated Folding Kinetics, R102H/G134S, Ph 8
1qrx: Crystal Structure of Wild-type Alpha-lytic Protease at 1.6 A, Ph 5.14
1ssx: 0.83a Resolution Crystal Structure of Alpha-lytic Protease at Ph 8
1tal: Alpha-lytic Protease at 120 K (single Structure Model)
2alp: Refined Structure of Alpha-lytic Protease at 1.7 Angstroms Resolution. Analysis of Hydrogen Bonding and Solvent Structure
2ull: Multiple Conformation Structure of Alpha-lytic Protease at 120 K
2lpr: Structural Basis for Broad Specificity in Alpha-lytic Protease Mutants
2h5c: 0.82a Resolution Crystal Structure of Alpha-lytic Protease at Ph 5
2h5d: 0.9a Resolution Crystal Structure of Alpha-lytic Protease Complexed with a Transition State Analogue, Meosuc-ala-ala- Pro-val Boronic Acid
3m7t: Crystal Structure of Alpha-lytic Protease Sb2+3 E8A/R105S Mutant
3m7u: Crystal Structure of Alpha-lytic Protease Sb1+2 R64A/E182Q Mutant
3qgj: 1.3a Structure of Alpha-lytic Protease Bound to Ac-alaalapro-alanal
3urc: T181G Mutant of Alpha-lytic Protease
3urd: T181A Mutant of Alpha-lytic Protease
3ure: Repack Mutant (T181I, W199L, Q210I) of Alpha-lytic Protease
5wot: Nmr Solution Structure of A-lytic Protease Using Two 4d-spectra