Structure of PDB 6vp5 Chain D

Receptor sequence
>6vp5D (length=331) Species: 319 (Pseudomonas savastanoi pv. phaseolicola) [Search protein sequence]
NLQTFELPTEVTGCAADISLGRALIQAWQKDGIFQIKTDSEQDRKTQEAM
AASKQFCKEPLTFKSSCVSDLTYSGYVASGEEVTAGKPDFPEIFTVCKDL
SVGDQRVKAGWPCHGPVPWPNNTYQKSMKTFMEELGLAGERLLKLTALGF
ELPINTFTDLTRDGWHHMRVLRFPPQTSTLSRGIGAHTEYGLLVIAAQDD
VGGLYIRPPVEGEKRNRNWLPGESSAGMFEHDEPWTFVTPTPGVWTVFPG
DILQFMTGGQLLSTPHKVKLNTRERFACAYFHEPNFEASAYPLFEPANER
IHYGEHFTNMFMRCYPDRITTQRINKENRLA
3D structure
PDB6vp5 An Iron(IV)-Oxo Intermediate Initiating l-Arginine Oxidation but Not Ethylene Production by the 2-Oxoglutarate-Dependent Oxygenase, Ethylene-Forming Enzyme.
ChainD
Resolution1.97 Å
3D
structure
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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).
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 FE D H189 E191 H268 H187 E189 H266
BS02 AKG D R171 L173 F175 E191 H268 V270 R277 A279 R169 L171 F173 E189 H266 V268 R275 A277
BS03 ARG D E84 T86 R171 H189 E191 Y192 R316 C317 E82 T84 R169 H187 E189 Y190 R313 C314
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:6vp5, PDBe:6vp5, PDBj:6vp5
PDBsum6vp5
PubMed33522811
UniProtP32021|EFE_PSESH 2-oxoglutarate-dependent ethylene/succinate-forming enzyme (Gene Name=efe)

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