Structure of PDB 5v34 Chain A Binding Site BS01

Receptor Information
>5v34 Chain A (length=342) Species: 319 (Pseudomonas savastanoi pv. phaseolicola) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMTNLQTFELPTEVTGCAADISLGRALIQAWQKDGIFQIKTDSEQDRKTQ
EAMAASKQFCKEPLTFKSSCVSDLTYSGYVASGEEVTAGKPDFPEIFTVC
KDLSVGDQRVKAGWPCHGPVPWPNNTYQKSMKTFMEELGLAGERLLKLTA
LGFELPINTFTDLTRDGWHHMRVLRFPPQTSTLSRGIGAHTDYGLLVIAA
QDDVGGLYIRPPVEGEKRNRNWLPGESSAGMFEHDEPWTFVTPTPGVWTV
FPGDILQFMTGGQLLSTPHKVKLNTRERFACAYFHEPNFEASAYPLFEPS
ANERIHYGEHFTNMFMRCYPDRITTQRINKENRLAHLEDLKK
Ligand information
Ligand IDARG
InChIInChI=1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/p+1/t4-/m0/s1
InChIKeyODKSFYDXXFIFQN-BYPYZUCNSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CC(C(=O)O)N)CNC(=[NH2+])N
CACTVS 3.341N[C@@H](CCCNC(N)=[NH2+])C(O)=O
OpenEye OEToolkits 1.5.0C(C[C@@H](C(=O)O)N)CNC(=[NH2+])N
CACTVS 3.341N[CH](CCCNC(N)=[NH2+])C(O)=O
ACDLabs 10.04O=C(O)C(N)CCCN\C(=[NH2+])N
FormulaC6 H15 N4 O2
NameARGININE
ChEMBL
DrugBank
ZINC
PDB chain5v34 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5v34 Structures and Mechanisms of the Non-Heme Fe(II)- and 2-Oxoglutarate-Dependent Ethylene-Forming Enzyme: Substrate Binding Creates a Twist.
Resolution1.48 Å
Binding residue
(original residue number in PDB)		E84 T86 R171 H189 D191 Y192 F314 R316 C317
Binding residue
(residue number reindexed from 1)		E85 T87 R172 H190 D192 Y193 F315 R317 C318
Annotation score5
Enzymatic activity
Enzyme Commision number 1.13.12.19: 2-oxoglutarate dioxygenase (ethylene-forming).
1.14.20.7: 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate- forming).
Gene Ontology
Molecular Function
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0102276 2-oxoglutarate oxygenase/decarboxylase (ethylene-forming) activity
Biological Process
GO:0009693 ethylene biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5v34, PDBe:5v34, PDBj:5v34
PDBsum5v34
PubMed28780854
UniProtP32021|EFE_PSESH 2-oxoglutarate-dependent ethylene/succinate-forming enzyme (Gene Name=efe)

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