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4R3V

Structure of karilysin propeptide and 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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AASP25
AHIS155
AHIS159
AHIS165
AHOH452

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 CA A 303
ChainResidue
AASP109
AGLY110
ATHR112
AILE114
AASP135
AGLU138

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
APRO28
ALEU29
ATHR30
AASN33
ATYR106
BASN34

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
ALYS41
ATRP42
AASN43
ALYS44
ALEU195
ATYR196
AGOL306
BASN101

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 306
ChainResidue
AASP194
AGLY197
AGOL305
BASN101

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BASP25
BHIS155
BHIS159
BHIS165

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS102
BASP104
BHIS117
BHIS133

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASP109
BGLY110
BTHR112
BILE114
BASP135
BGLU138

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
AALA156
BALA156

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

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PDB entries from 2024-10-30

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