Structure of PDB 5lun Chain D Binding Site BS01

Receptor Information
>5lun Chain D (length=341) Species: 319 (Pseudomonas savastanoi pv. phaseolicola) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NTNLQTFELPTEVTGCAADISLGRALIQAWQKDGIFQIKTDSEQDRKTQE
AMAASKQFCKEPLTFKSSCVSDLTYSGYVASGEEVTAGKPDFPEIFTVCK
DLSVGDQRVKAGWPCHGPVPWPNNTYQKSMKTFMEELGLAGERLLKLTAL
GFELPINTFTDLTRDGWHHMRVLRFPPQTSTLSRGIGAHTDYGLLVIAAQ
DDVGGLYIRPPVEGEKRNRNWLPGESSAGMFEHDEPWTFVTPTPGVWTVF
PGDILQFMTGGQLLSTPHKVKLNTRERFACAYFHEPNFEASAYPLFEPSA
NERIHYGEHFTNMFMRCYPDRITTQRINKENRLAHLEDLKK
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain5lun Chain D Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5lun Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate.
Resolution1.08 Å
Binding residue
(original residue number in PDB)		H189 D191 H268
Binding residue
(residue number reindexed from 1)		H189 D191 H268
Annotation score1
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5lun, PDBe:5lun, PDBj:5lun
PDBsum5lun
PubMed28420789
UniProtP32021|EFE_PSESH 2-oxoglutarate-dependent ethylene/succinate-forming enzyme (Gene Name=efe)

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