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6DWV

Crystal structure of the LigJ Hydratase in the Apo state

Functional Information from GO Data
ChainGOidnamespacecontents
A0009056biological_processcatabolic process
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0046274biological_processlignin catabolic process
A0046872molecular_functionmetal ion binding
B0009056biological_processcatabolic process
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0016831molecular_functioncarboxy-lyase activity
B0046274biological_processlignin catabolic process
B0046872molecular_functionmetal ion binding
C0009056biological_processcatabolic process
C0016787molecular_functionhydrolase activity
C0016829molecular_functionlyase activity
C0016831molecular_functioncarboxy-lyase activity
C0046274biological_processlignin catabolic process
C0046872molecular_functionmetal ion binding
D0009056biological_processcatabolic process
D0016787molecular_functionhydrolase activity
D0016829molecular_functionlyase activity
D0016831molecular_functioncarboxy-lyase activity
D0046274biological_processlignin catabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS8
BHIS10
BHIS178
BGLU284
BHOH573

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS8
AHIS10
AHIS178
AHOH559

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN C 401
ChainResidue
CHIS8
CHIS10
CHIS178
CHOH565

site_idAC4
Number of Residues3
Detailsbinding site for residue ZN D 401
ChainResidue
DHIS8
DHIS10
DHIS178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:30207699
ChainResidueDetails
BGLU284
AGLU284
CGLU284
DGLU284

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:30207699, ECO:0000312|PDB:6DWV
ChainResidueDetails
BHIS8
DHIS8
DHIS10
DHIS178
BHIS10
BHIS178
AHIS8
AHIS10
AHIS178
CHIS8
CHIS10
CHIS178

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:30207699, ECO:0000312|PDB:6DXS
ChainResidueDetails
BARG71
CTYR194
CHIS223
CARG290
DARG71
DTYR194
DHIS223
DARG290
BTYR194
BHIS223
BARG290
AARG71
ATYR194
AHIS223
AARG290
CARG71

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PDB entries from 2024-07-17

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