Structure of PDB 2wbo Chain A

Receptor sequence
>2wboA (length=336) Species: 1960 (Streptomyces vinaceus) [Search protein sequence]
VRPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRR
LRTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFL
LMLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTE
DAFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIR
PDDSHLQVNNSTAQQGRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGD
FSAPAEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRA
FQPRYDGRDRWLKRINITRDLHRSRKAWAGDSRVLG
3D structure
PDB2wbo Structural Basis for the Erythro-Stereospecificity of the L-Arginine Oxygenase Vioc in Viomycin Biosynthesis.
ChainA
Resolution1.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.41: L-arginine hydroxylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ARG A Q137 L156 V157 S158 E170 D222 S224 D268 R334 A347 G356 Q117 L136 V137 S138 E150 D202 S204 D248 R314 A327 G336
BS02 FE2 A H168 E170 H316 H148 E150 H296
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0046872 metal ion binding
GO:0102525 2-oxoglutarate, L-arginine oxygenase (succinate-forming) activity
Biological Process
GO:0017000 antibiotic biosynthetic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2wbo, PDBe:2wbo, PDBj:2wbo
PDBsum2wbo
PubMed19490124
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

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