Structure of PDB 3ovr Chain B Binding Site BS01
Receptor Information
>3ovr Chain B (length=220) Species:
9606
(Homo sapiens) [
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GCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPV
VESLRKQLGQDPFFDMHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGA
LIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFM
EDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRS
EDPRSVINLLRNVCSEAAQK
Ligand information
Ligand ID
FE2
InChI
InChI=1S/Fe/q+2
InChIKey
CWYNVVGOOAEACU-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Fe+2]
CACTVS 3.341
[Fe++]
Formula
Fe
Name
FE (II) ION
ChEMBL
DrugBank
DB14510
ZINC
PDB chain
3ovr Chain B Residue 229 [
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Receptor-Ligand Complex Structure
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PDB
3ovr
Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE
Resolution
1.948 Å
Binding residue
(original residue number in PDB)
H35 D37 H70 D175
Binding residue
(residue number reindexed from 1)
H32 D34 H67 D172
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
S10 H35 D37 M39 H70 M72 M141 D175
Catalytic site (residue number reindexed from 1)
S7 H32 D34 M36 H67 M69 M138 D172
Enzyme Commision number
5.1.3.1
: ribulose-phosphate 3-epimerase.
Gene Ontology
Molecular Function
GO:0004750
D-ribulose-phosphate 3-epimerase activity
GO:0005515
protein binding
GO:0016853
isomerase activity
GO:0016857
racemase and epimerase activity, acting on carbohydrates and derivatives
GO:0042802
identical protein binding
GO:0042803
protein homodimerization activity
GO:0046872
metal ion binding
Biological Process
GO:0005975
carbohydrate metabolic process
GO:0006098
pentose-phosphate shunt
GO:0009052
pentose-phosphate shunt, non-oxidative branch
Cellular Component
GO:0005829
cytosol
GO:0070062
extracellular exosome
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:3ovr
,
PDBe:3ovr
,
PDBj:3ovr
PDBsum
3ovr
PubMed
20923965
UniProt
Q96AT9
|RPE_HUMAN Ribulose-phosphate 3-epimerase (Gene Name=RPE)
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