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4IN9

Structure of karilysin MMP-like catalytic domain in complex with inhibitory tetrapeptide SWFP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS155
AHIS159
AHIS165
BSER1

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHIS102
AASP104
AHIS117
AHIS133

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 303
ChainResidue
ASER78
ALEU80
AHOH536
AHOH537
AHOH538
ASER75

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 304
ChainResidue
APHE108
AGOL307
AHOH427
AHOH478
AHOH548
AHOH595

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
ASER75
ASER81
APHE82
AHOH438
AHOH535

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 306
ChainResidue
AALA118
AGLN183
AHOH569
AHOH594
AHOH605
BSER1

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
AASP135
AASP137
AGLU138
ANA304
AHOH596

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 308
ChainResidue
ATYR52
ALYS94
ALYS96
AHIS131
ALEU132
AHIS133
AHOH547
AHOH600

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 309
ChainResidue
AASP104
AGLY105
ATYR128
ASER169
ASER170
AHOH487
AHOH513
AHOH580

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEIGHLL
ChainResidueDetails
AVAL152-LEU161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:23695557
ChainResidueDetails
AGLU156

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:23695557
ChainResidueDetails
AHIS102
AASP104
AHIS117
AHIS133
AHIS155
AHIS159
AHIS165

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PDB entries from 2024-08-21

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