Structure of PDB 2bes Chain D

Receptor sequence

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

SGMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCI
AAATRTVADPGSLGIVLGGSGNGEQIAANKVPGARCALAWSVQTAALARE
HNNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYERT
HEAPPVP

3D structure

• PDB: 2bes Competitive Inhibitors of Mycobacterium Tuberculosis Ribose-5-Phosphate Isomerase B Reveal New Information About the Reaction Mechanism.
• Chain: D
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D11 G69 S71 H102 H138
• Catalytic site (residue number reindexed from 1): D10 G68 S70 H101 H137
• 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	RES	D	H102 R137 R141	H101 R136 R140	MOAD: Ki=0.057mM BindingDB: Ki=57000nM
BS02	RES	D	D11 H12 G70 S71 G74 E75 R113	D10 H11 G69 S70 G73 E74 R112	MOAD: Ki=0.057mM BindingDB: Ki=57000nM

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