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2XS4

Structure of karilysin catalytic MMP domain in complex with magnesium

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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 997
ChainResidue
ASER75
ASER78
AHOH2070
AHOH2072
AHOH2192

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 998
ChainResidue
AHIS102
AASP104
AHIS117
AHIS133

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
AHIS155
AHIS159
AHIS165
BALA301

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 1202
ChainResidue
AASN87
AASN143
AGLY144
ASER145
AHOH2132

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

237735

PDB entries from 2025-06-18

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