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1FY8

CRYSTAL STRUCTURE OF THE DELTAILE16VAL17 RAT ANIONIC TRYPSINOGEN-BPTI COMPLEX

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
EHOH524

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 I 990
ChainResidue
IHOH661
IGLU7
IARG42
IHOH538

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 I 991
ChainResidue
EGLN239
IARG20
ITYR35
IHOH611
IHOH717

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 I 992
ChainResidue
ELYS60
IARG20

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

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
EASP189-VAL200

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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