Structure of PDB 5v31 Chain A Binding Site BS02
Receptor Information
>5v31 Chain A (length=340) Species:
319
(Pseudomonas savastanoi pv. phaseolicola) [
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NLQTFELPTEVTGCAADISLGRALIQAWQKDGIFQIKTDSEQDRKTQEAM
AASKQFCKEPLTFKSSCVSDLTYSGYVASGEEVTAGKPDFPEIFTVCKDL
SVGDQRVKAGWPCHGPVPWPNNTYQKSMKTFMEELGLAGERLLKLTALGF
ELPINTFTDLTRDGWHHMRVLRFPPQTSTLSRGIGAHTDYGLLVIAAQDD
VGGLYIRPPVEGEKRNRNWLPGESSAGMFEHDEPWTFVTPTPGVWTVFPG
DILQFMTGGQLLSTPHKVKLNTRERFACAYFHEPNFEASAYPLFEPSANE
RIHYGEHFTNMFMRCYPDRITTQRINKENRLAHLEDLKKY
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
5v31 Chain A Residue 402 [
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Receptor-Ligand Complex Structure
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PDB
5v31
Structures and Mechanisms of the Non-Heme Fe(II)- and 2-Oxoglutarate-Dependent Ethylene-Forming Enzyme: Substrate Binding Creates a Twist.
Resolution
2.45 Å
Binding residue
(original residue number in PDB)
H189 D191 H268
Binding residue
(residue number reindexed from 1)
H187 D189 H266
Annotation score
1
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:5v31
,
PDBe:5v31
,
PDBj:5v31
PDBsum
5v31
PubMed
28780854
UniProt
P32021
|EFE_PSESH 2-oxoglutarate-dependent ethylene/succinate-forming enzyme (Gene Name=efe)
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