Structure of PDB 1amk Chain A

Receptor sequence

>1amkA (length=250) Species: 5665 (Leishmania mexicana)

SAKPQPIAAANWKCNGTTASIEKLVQVFNEHTISHDVQCVVAPTFVHIPL
VQAKLRNPKYVISAENAIAKSGAFTGEVSMPILKDIGVHWVILGHSERRT
YYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAI
AAKLTKDAWNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGT
DVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPEFRDIIDATR

3D structure

• PDB: 1amk Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.
• Chain: A
• Resolution: 1.83 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N11 K13 H95 E97 E167 G173 S213
• Catalytic site (residue number reindexed from 1): N11 K13 H95 E97 E167 G173 S213
• 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 G173 G212 S213 G234 G235	K13 H95 E167 I172 G173 G212 S213 G234 G235	MOAD: Ki=0.05mM PDBbind-CN: -logKd/Ki=4.30,Ki=50uM

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:1amk, PDBe:1amk, PDBj:1amk
• PDBsum: 1amk
• PubMed: 10235625
• UniProt: P48499|TPIS_LEIME Triosephosphate isomerase