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6GPE

Crystal Structure of the CsiD Glutarate Hydroxylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0008198molecular_functionferrous iron binding
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
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 Residues6
Detailsbinding site for residue FE2 A 401
ChainResidue
AHIS160
AASP162
AHIS292
AHOH616
AHOH690
AHOH706

site_idAC2
Number of Residues6
Detailsbinding site for residue FE2 B 401
ChainResidue
BHOH595
BHOH713
BHOH733
BHIS160
BASP162
BHIS292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11910018, ECO:0000269|PubMed:30498244, ECO:0000312|PDB:1JR7, ECO:0000312|PDB:6GPE
ChainResidueDetails
AHIS160
AASP162
AHIS292
BHIS160
BASP162
BHIS292

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PDB entries from 2024-07-24

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