Structure of PDB 3ovr Chain B

Receptor sequence

>3ovrB (length=220) Species: 9606 (Homo sapiens)

GCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPV
VESLRKQLGQDPFFDMHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGA
LIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFM
EDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRS
EDPRSVINLLRNVCSEAAQK

3D structure

• PDB: 3ovr Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE
• Chain: B
• Resolution: 1.948 Å

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.

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	FE2	B	H35 D37 H70 D175	H32 D34 H67 D172
BS02	5SP	B	L12 H35 D37 H70 M72 P145 G149 D175 G176 G177 G197 S198	L9 H32 D34 H67 M69 P142 G146 D172 G173 G174 G194 S195

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

External links

• PDB: RCSB:3ovr, PDBe:3ovr, PDBj:3ovr
• PDBsum: 3ovr
• PubMed: 20923965
• UniProt: Q96AT9|RPE_HUMAN Ribulose-phosphate 3-epimerase (Gene Name=RPE)