Structure of PDB 2vxn Chain A

Receptor sequence

>2vxnA (length=249) Species: 5665 (Leishmania mexicana)

AKPQPIAAANWKCNGTTASIEKLVQVFNEHTISHDVQCVVAPTFVHIPLV
QAKLRNPKYVISAQNAIAKSGAFTGEVSMPILKDIGVHWVILGHSERRTY
YGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIA
AKLTKDAWNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTD
VAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPEFRDIIDATR

3D structure

• PDB: 2vxn Atomic Resolution Crystallography of a Complex of Triosephosphate Isomerase with a Reaction-Intermediate Analog: New Insight in the Proton Transfer Reaction Mechanism.
• Chain: A
• Resolution: 0.82 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	PGH	A	K13 H95 E167 I172 G173 G212 S213 L232 G234 G235	K12 H94 E166 I171 G172 G211 S212 L231 G233 G234	PDBbind-CN: -logKd/Ki=5.00,Kd=10uM
BS02	PGA	A	K13 H95 E167 I172 G173 G212 S213 G234 G235	K12 H94 E166 I171 G172 G211 S212 G233 G234

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:2vxn, PDBe:2vxn, PDBj:2vxn
• PDBsum: 2vxn
• PubMed: 20235230
• UniProt: P48499|TPIS_LEIME Triosephosphate isomerase