Structure of PDB 2vvq Chain A

Receptor sequence

>2vvqA (length=156) Species: 83332 (Mycobacterium tuberculosis H37Rv)

GMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIA
AATRTVADPGSLGIVLGGSGNGEQIAANKVPGARCALAWSVQTAALAREH
NNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYERTH
EAPPVP

3D structure

• PDB: 2vvq D-Ribose-5-Phosphate Isomerase B from Escherichia Coli is Also a Functional D-Allose-6-Phosphate Isomerase, While the Mycobacterium Tuberculosis Enzyme is not.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D11 G69 S71 H102 H138
• Catalytic site (residue number reindexed from 1): D9 G67 S69 H100 H136
• Enzyme Commision number: 5.3.1.6: ribose-5-phosphate isomerase.

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	R10	A	D11 H12 Y46 G69 G70 S71 G72 G74 E75 R113	D9 H10 Y44 G67 G68 S69 G70 G72 E73 R111
BS02	R10	A	H102 R137 R141	H100 R135 R139

Gene Ontology

Molecular Function

• GO:0004751 ribose-5-phosphate isomerase activity
• GO:0005515 protein binding
• GO:0016853 isomerase activity
• GO:0016861 intramolecular oxidoreductase activity, interconverting aldoses and ketoses

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0006098 pentose-phosphate shunt
• GO:0009052 pentose-phosphate shunt, non-oxidative branch
• GO:0019316 D-allose catabolic process

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:2vvq, PDBe:2vvq, PDBj:2vvq
• PDBsum: 2vvq
• PubMed: 18640127
• UniProt: P9WKD7|RPIB_MYCTU Ribose-5-phosphate isomerase B (Gene Name=rpiB)