Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4ISO

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 Residues9
DetailsBINDING SITE FOR RESIDUE GSH A 301
ChainResidue
ATRP29
ATYR114
AARG119
APRO120
ACYS122
AARG206
AILE207
AHOH462
AHOH535

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
APHE130
AVAL162
AILE163
AGLN164
AGLN165
AMET181
AARG230
AHOH447
BGLU272
BHOH531

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AHIS57
ACYS58
ATYR59
AILE60
AASP60
ATYR60
AHOH472
BPHE263
BARG265
BTYR280
BGLY282

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 304
ChainResidue
ALEU36
ATHR65
AARG84
AHOH460

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PEG A 305
ChainResidue
AASP23
AGLU24
AGLY25
AGLU26
ATRP27
APRO28
AHIS71
AMET117
ALEU155
AHOH465

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 306
ChainResidue
ASER186
AGLY187
AALA221
AGLN221
AARG222

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 401
ChainResidue
ALEU36
AGLY37
BLEU291
BARG292

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B 402
ChainResidue
BGLY285
BLYS287

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon