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9BWU

Glutarate L-2-hydroxylase (CsiD/GlaH) from Escherichia coli at 2.20 Angstroms Resolution

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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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