Structure of PDB 2wbp Chain A

Receptor sequence
>2wbpA (length=332) Species: 1960 (Streptomyces vinaceus) [Search protein sequence]
VRPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRR
LRTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFL
LMLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTE
DAFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIR
PDDSHLQVNNSTRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDFSAP
AEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAFQPR
YDGRDRWLKRINITRDLHRSRKAWAGDSRVLG
3D structure
PDB2wbp Structural Basis for the Erythro-Stereospecificity of the L-Arginine Oxygenase Vioc in Viomycin Biosynthesis.
ChainA
Resolution1.16 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 R47 Y48 E55 D59 G356 R27 Y28 E35 D39 G332
BS02 FE2 A H168 E170 H316 H148 E150 H292
BS03 ZZU A Q137 L156 V157 S158 L165 H168 D222 S224 D268 D270 R334 Q117 L136 V137 S138 L145 H148 D202 S204 D244 D246 R310
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:2wbp, PDBe:2wbp, PDBj:2wbp
PDBsum2wbp
PubMed19490124
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

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