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2XS3

Structure of karilysin catalytic MMP domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 998
ChainResidue
AHIS102
AASP104
AHIS117
AHIS133

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
AHIS155
AHIS159
AHIS165
CALA201

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 998
ChainResidue
BASP104
BHIS117
BHIS133
BHIS102

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 999
ChainResidue
BHIS155
BHIS159
BHIS165
DALA201

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TRS B 1305
ChainResidue
BTYR106
BALA118
BPHE119
BGLN183

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:23695557
ChainResidueDetails
AGLU156
BGLU156

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:23695557
ChainResidueDetails
AHIS102
BHIS117
BHIS133
BHIS155
BHIS159
BHIS165
AASP104
AHIS117
AHIS133
AHIS155
AHIS159
AHIS165
BHIS102
BASP104

226707

PDB entries from 2024-10-30

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