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4ISL

Crystal Structure of the inactive 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 Residues5
DetailsBINDING SITE FOR RESIDUE PG4 B 401
ChainResidue
ALEU36
AGLY37
BLEU291
BARG292
BHOH531

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AGLN165
AMET181
AARG230
BGLU272
BHOH527
APHE130
AVAL162
AILE163
AGLN164

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AHIS57
ACYS58
ATYR59
AILE60
AASP60
BPHE263
BARG265
BTYR280
BGLY282

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE A 303
ChainResidue
AGLN145
ASER186
AGLY187
AALA221

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AGLU26
ATRP137
ALYS157
AHOH469

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GSH A 305
ChainResidue
ATRP29
AARG119
APRO120
AILE121
ACYS122
AARG206
AILE207

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

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 Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
AALA195

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

227344

PDB entries from 2024-11-13

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