Structure of PDB 2vvo Chain D

Receptor sequence

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

GMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIA
AATRTVADPGSLGIVLGGSGNGEQIAANKVPGARCALAWSVQTAALAREH
NNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYERTH
EAPPVP

3D structure

• PDB: 2vvo 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: D
• Resolution: 1.85 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	A6P	D	H102 N103 R137 R141	H100 N101 R135 R139	MOAD: ic50=6.3mM
BS02	A6P	D	D11 H12 Y46 G69 G70 S71 G74 E75 R113	D9 H10 Y44 G67 G68 S69 G72 E73 R111	MOAD: ic50=6.3mM

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