Structure of PDB 2bet Chain A

Receptor sequence

>2betA (length=157) Species: 83332 (Mycobacterium tuberculosis H37Rv)

GMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIA
AATRTVADPGSLGIVLGGSGNGEQIAANKVPGARCALAWSVQTAALAREH
NNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYERTH
EAPPVPG

3D structure

• PDB: 2bet Competitive Inhibitors of Mycobacterium Tuberculosis Ribose-5-Phosphate Isomerase B Reveal New Information About the Reaction Mechanism
• Chain: A
• Resolution: 2.2 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	DEZ	A	D11 H12 G70 S71 G74 E75	D9 H10 G68 S69 G72 E73	MOAD: Ki=1.7mM PDBbind-CN: -logKd/Ki=2.77,Ki=1.7mM
BS02	DEZ	A	H102 R137 R141	H100 R135 R139	MOAD: Ki=1.7mM PDBbind-CN: -logKd/Ki=2.77,Ki=1.7mM

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:2bet, PDBe:2bet, PDBj:2bet
• PDBsum: 2bet
• PubMed: 15590681
• UniProt: P9WKD7|RPIB_MYCTU Ribose-5-phosphate isomerase B (Gene Name=rpiB)