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6HL9

Crystal Structure of the CsiD Glutarate Hydroxylase in complex with Succinate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0019477biological_processL-lysine catabolic process
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0050498molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with 2-oxoglutarate as one donor, and the other dehydrogenated
A0051213molecular_functiondioxygenase activity
A0090549biological_processresponse to carbon starvation
A0106343molecular_functionglutarate dioxygenase activity
B0005506molecular_functioniron ion binding
B0008198molecular_functionferrous iron binding
B0016491molecular_functionoxidoreductase activity
B0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
B0019477biological_processL-lysine catabolic process
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0050498molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with 2-oxoglutarate as one donor, and the other dehydrogenated
B0051213molecular_functiondioxygenase activity
B0090549biological_processresponse to carbon starvation
B0106343molecular_functionglutarate dioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue FE2 A 401
ChainResidue
AHIS160
AASP162
AHIS292
ASIN402

site_idAC2
Number of Residues6
Detailsbinding site for residue SIN A 402
ChainResidue
AHOH577
ATYR149
AHIS160
AARG305
AFE2401
AHOH501

site_idAC3
Number of Residues4
Detailsbinding site for residue FE2 B 401
ChainResidue
BHIS160
BASP162
BHIS292
BSIN402

site_idAC4
Number of Residues6
Detailsbinding site for residue SIN B 402
ChainResidue
BMET157
BHIS160
BHIS292
BARG294
BARG305
BFE2401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11910018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30498244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JR7","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6GPE","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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