Structure of PDB 2y62 Chain A

Receptor sequence

>2y62A (length=249) Species: 5665 (Leishmania mexicana)

AKPQPIAAANWKCNGTTASIEKLVQVFNEHTISHDVQCVVAPTFVHIPLV
QAKLRNPKYVISAQNAIAKSGAFTGEVSMPILKDIGVHWVILGHSERRTY
YGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIA
AKLTKDAWNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTD
VAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPEFRDIIDATR

3D structure

• PDB: 2y62 High Resolution Crystal Structures of Triosephosphate Isomerase Complexed with its Suicide Inhibitors: The Conformational Flexibility of the Catalytic Glutamate in its Closed, Liganded Active Site.
• Chain: A
• Resolution: 1.08 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N1011 K1013 H1095 E1097 E1167 G1173 S1213
• 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	G3P	A	K1013 H1095 E1167 I1172 G1173 G1212 S1213 L1232 G1234 G1235	K12 H94 E166 I171 G172 G211 S212 L231 G233 G234
BS02	1GP	A	K1013 H1095 E1167 I1172 G1173 G1212 S1213 L1232 G1234 G1235	K12 H94 E166 I171 G172 G211 S212 L231 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:2y62, PDBe:2y62, PDBj:2y62
• PDBsum: 2y62
• PubMed: 21633986
• UniProt: P48499|TPIS_LEIME Triosephosphate isomerase