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4ISN

Crystal Structure of Matriptase in complex with its inhibitor HAI-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 B 401
ChainResidue
ALEU36
AGLY37
BARG292
BHOH520

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GSH A 301
ChainResidue
AILE207
AHOH463
AHOH469
ATRP29
AARG119
APRO120
ACYS122
AARG206

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLS
ChainResidueDetails
AASP189-SER200

site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGClgnknnYlreeeC
ChainResidueDetails
BPHE278-CYS296

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond => ECO:0000250
ChainResidueDetails
BARG260
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLN164

237735

PDB entries from 2025-06-18

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