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7QIQ

CRYSTAL STRUCTURE OF THE P1 aminobutanoic acid (ABU) BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0004867molecular_functionserine-type endopeptidase inhibitor activity
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004252molecular_functionserine-type endopeptidase activity
G0006508biological_processproteolysis
H0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
BVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV
ChainResidueDetails
CSER189-VAL200

site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCrakrnnFksaedC
ChainResidueDetails
DPHE33-CYS51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Reactive bond for trypsin
ChainResidueDetails
DABA15
HABA15
FHIS57
FASP102

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 387
ChainResidueDetails
CGLY193electrostatic stabiliser
CSER195covalent catalysis
CGLY196electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 387
ChainResidueDetails
GGLY193electrostatic stabiliser
GSER195covalent catalysis
GGLY196electrostatic stabiliser

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PDB entries from 2024-07-17

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