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3TGK

TRYPSINOGEN MUTANT D194N AND DELETION OF ILE 16-VAL 17 COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI)

Functional Information from GO Data
ChainGOidnamespacecontents
E0004252molecular_functionserine-type endopeptidase activity
E0006508biological_processproteolysis
I0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 500
ChainResidue
EGLU70
EASN72
EVAL75
EGLU77
EGLU80
EHOH513

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 I 990
ChainResidue
IPHE4
IARG42
IHOH538

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 I 991
ChainResidue
EGLN239
IARG20
ITYR35
IHOH636
IHOH671

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 I 992
ChainResidue
ELYS60
IILE18
IARG20
ILYS46

site_idCAT
Number of Residues3
DetailsTHE CATALYTIC TRIAD
ChainResidue
EHIS57
EASP102
ESER195

Functional Information from PROSITE/UniProt
site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCrakrnnFksaedC
ChainResidueDetails
IPHE33-CYS51

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
EVAL53-CYS58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond for trypsin
ChainResidueDetails
ILYS15
EMET104
EGLY197

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
EASN72
EASN74
EGLU77
EPHE82

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Required for specificity => ECO:0000250
ChainResidueDetails
ECYS191

218853

PDB entries from 2024-04-24

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