Structure of PDB 2wbp Chain A Binding Site BS03

Receptor Information
>2wbp Chain A (length=332) Species: 1960 (Streptomyces vinaceus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VRPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRR
LRTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFL
LMLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTE
DAFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIR
PDDSHLQVNNSTRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDFSAP
AEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAFQPR
YDGRDRWLKRINITRDLHRSRKAWAGDSRVLG
Ligand information
Ligand IDZZU
InChIInChI=1S/C6H14N4O3/c7-4(5(12)13)3(11)1-2-10-6(8)9/h3-4,11H,1-2,7H2,(H,12,13)(H4,8,9,10)/t3-,4-/m0/s1
InChIKeyVIDUVSPOWYVZIC-IMJSIDKUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.6.1C(CNC(=N)N)C(C(C(=O)O)N)O
ACDLabs 10.04O=C(O)C(N)C(O)CCNC(=[N@H])N
CACTVS 3.352N[CH]([CH](O)CCNC(N)=N)C(O)=O
CACTVS 3.352N[C@@H]([C@@H](O)CCNC(N)=N)C(O)=O
OpenEye OEToolkits 1.6.1C(CNC(=N)N)[C@@H]([C@@H](C(=O)O)N)O
FormulaC6 H14 N4 O3
Name(2S,3S)-3-HYDROXYARGININE
ChEMBL
DrugBank
ZINCZINC000013352215
PDB chain2wbp Chain A Residue 1359 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2wbp Structural Basis for the Erythro-Stereospecificity of the L-Arginine Oxygenase Vioc in Viomycin Biosynthesis.
Resolution1.16 Å
Binding residue
(original residue number in PDB)
Q137 L156 V157 S158 L165 H168 D222 S224 D268 D270 R334
Binding residue
(residue number reindexed from 1)
Q117 L136 V137 S138 L145 H148 D202 S204 D244 D246 R310
Annotation score5
Enzymatic activity
Enzyme Commision number 1.14.11.41: L-arginine hydroxylase.
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
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)

[Back to BioLiP]