	Home \| Site Map \| Copyright \| Contact us \| Privacy \|

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 3.4.21.14 - obsolete, reclassified now as EC 3.4.21.62 - EC 3.4.21.65 and EC 3.4.21.67

3D structures of EC 3.4.21.14 in Protein Data Bank

updated: 6 January 2022, 2:15

In total: 15 PDB structures of EC 3.4.21.14:

1mee: The Complex between The Subtilisin from a Mesophilic Bacterium and The Leech Inhibitor Eglin-c
1s02: Effects of Engineered Salt Bridges on The Stability of Subtilisin Bpn'
1sbt: Atomic Coordinates for Subtilisin Bpn (or Novo)
1st2: The Three-dimensional Structure of Bacillus Amyloliquefaciens Subtilisin at 1.8 Angstroms and an Analysis of The Structural Consequences of Peroxide Inactivation
1yja: Subtilisin Bpn' 8397+1 (e.c. 3.4.21.14) (mutant with Met 50 Replaced by Phe, Asn 76 Replaced by Asp, Gly 169 Replaced by Ala, Gln 206 Replaced by Cys, Asn 218 Replaced by Ser and Lys 256 Replaced by Tyr) (M50F, N76D, G169A, Q206C, N218S, and K256Y) in 20% Dimethylformamide
1yjb: Subtilisin Bpn' 8397+1 (e.c. 3.4.21.14) (mutant with Met 50 Replaced by Phe, Asn 76 Replaced by Asp, Gly 169 Replaced by Ala, Gln 206 Replaced by Cys, Asn 218 Replaced by Ser and Lys 256 Replaced by Tyr) (M50F, N76D, G169A, Q206C, N218S, and K256Y) in 35% Dimethylformamide
1yjc: Subtilisin Bpn' 8397+1 (e.c. 3.4.21.14) (mutant with Met 50 Replaced by Phe, Asn 76 Replaced by Asp, Gly 169 Replaced by Ala, Gln 206 Replaced by Cys, Asn 218 Replaced by Ser and Lys 256 Replaced by Tyr) (M50F, N76D, G169A, Q206C, N218S, and K256Y) in 50% Dimethylformamide
2st1: The Three-dimensional Structure of Bacillus Amyloliquefaciens Subtilisin at 1.8 Angstroms and an Analysis of The Structural Consequences of Peroxide Inactivation
2sni: Structural Comparison of Two Serine Proteinase-protein Inhibitor Complexes. Eglin-c-subtilisin Carlsberg and Ci-2- Subtilisin Novo
2sic: Refined Crystal Structure of The Complex of Subtilisin Bpn' and Streptomyces Subtilisin Inhibitor at 1.8 Angstroms Resolution
2sbt: A Comparison of The Three-dimensional Structures of Subtilisin Bpn and Subtilisin Novo
2prk: Synchrotron X-ray Data Collection and Restrained Least- Squares Refinement of The Crystal Structure of Proteinase K at 1.5 Angstroms Resolution
5ffn: Complex of Subtilase Subty from Bacillus Sp. Ty145 with Chymotrypsin Inhibitor CI2A
5fbz: Structure of Subtilase Subhal from Bacillus Halmapalus - Complex with Chymotrypsin Inhibitor CI2A
5fax: Structure of Subtilase Subhal from Bacillus Halmapalus