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6DXQ

Crystal structure of the LigJ Hydratase product complex with 4-carboxy-4-hydroxy-2-oxoadipate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0019748biological_processsecondary metabolic process
A0046274biological_processlignin catabolic process
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0016831molecular_functioncarboxy-lyase activity
B0019748biological_processsecondary metabolic process
B0046274biological_processlignin catabolic process
B0046872molecular_functionmetal ion binding
C0005737cellular_componentcytoplasm
C0016787molecular_functionhydrolase activity
C0016829molecular_functionlyase activity
C0016831molecular_functioncarboxy-lyase activity
C0019748biological_processsecondary metabolic process
C0046274biological_processlignin catabolic process
C0046872molecular_functionmetal ion binding
D0005737cellular_componentcytoplasm
D0016787molecular_functionhydrolase activity
D0016829molecular_functionlyase activity
D0016831molecular_functioncarboxy-lyase activity
D0019748biological_processsecondary metabolic process
D0046274biological_processlignin catabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS8
AHIS10
AHIS178
A7QD402

site_idAC2
Number of Residues15
Detailsbinding site for residue 7QD A 402
ChainResidue
AHIS178
ATYR194
AHIS223
AGLU284
AGLY287
AALA288
AARG290
AZN401
AHOH504
CARG234
AHIS8
AHIS10
AARG71
AALA72
ASER73

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS8
BHIS10
BHIS178
B7QD402

site_idAC4
Number of Residues13
Detailsbinding site for residue 7QD B 402
ChainResidue
BHIS8
BHIS10
BARG71
BALA72
BSER73
BHIS178
BTHR190
BTYR194
BHIS223
BGLU284
BALA288
BARG290
BZN401

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN C 401
ChainResidue
CHIS8
CHIS10
CHIS178
CGLU284
C7QD402

site_idAC6
Number of Residues15
Detailsbinding site for residue 7QD C 402
ChainResidue
AARG234
CHIS8
CHIS10
CARG71
CALA72
CSER73
CHIS178
CTYR194
CHIS223
CGLU284
CGLY287
CALA288
CARG290
CZN401
CHOH504

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN D 401
ChainResidue
DHIS8
DHIS10
DHIS178
D7QD402

site_idAC8
Number of Residues13
Detailsbinding site for residue 7QD D 402
ChainResidue
DHIS8
DHIS10
DTHR12
DARG71
DALA72
DSER73
DHIS178
DTYR194
DHIS223
DGLU284
DGLY287
DALA288
DZN401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"30207699","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30207699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6DWV","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30207699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6DXS","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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