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9EQF

Crystal structure of the L-arginine hydroxylase VioC MeHis316, bound to Fe(II), L-arginine, and succinate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0017000biological_processantibiotic biosynthetic process
A0046872molecular_functionmetal ion binding
A0102525molecular_function2-oxoglutarate, L-arginine oxygenase (succinate-forming) activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ALEU117-ALA135

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ALEU156
AHIS168
AGLU170
ATHR194
AASP268
AMHS316
AARG330
AARG334

237992

PDB entries from 2025-06-25

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