Structure of PDB 2v2c Chain A

Receptor sequence

>2v2cA (length=249) Species: 5702 (Trypanosoma brucei brucei)

SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMT
KERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAY
YGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIA
KKLKKADWAKVVIAYEPVWAIGTGKVLTPQQAQEAHALIRSWVSSKIGAD
VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ

3D structure

• PDB: 2v2c Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed-Like Conformation in Dimeric and Monomeric Tim.
• Chain: A
• Resolution: 1.89 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N11 K13 H95 E97 E167 G173 S213
• Catalytic site (residue number reindexed from 1): N10 K12 H94 E96 E166 G172 S212
• Enzyme Commision number: 5.3.1.1: triose-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	PGA	A	K13 H95 E167 I172 G212 S213 G234 G235	K12 H94 E166 I171 G211 S212 G233 G234	MOAD: Ki=0.39mM PDBbind-CN: -logKd/Ki=3.41,Ki=0.39mM

Gene Ontology

Molecular Function

• GO:0004807 triose-phosphate isomerase activity
• GO:0016853 isomerase activity

Biological Process

• GO:0006094 gluconeogenesis
• GO:0006096 glycolytic process
• GO:0019563 glycerol catabolic process
• GO:0046166 glyceraldehyde-3-phosphate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0020015 glycosome

External links

• PDB: RCSB:2v2c, PDBe:2v2c, PDBj:2v2c
• PDBsum: 2v2c
• PubMed: 18219118
• UniProt: P04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal