Structure of PDB 1qds Chain A

Receptor sequence
>1qdsA (length=250) Species: 5665 (Leishmania mexicana) [Search protein sequence]
SAKPQPIAAANWKCNGTTASIEKLVQVFNEHTISHDVQCVVAPTFVHIPL
VQAKLRNPKYVISAQNAIAKSGAFTGEVSMPILKDIGVHWVILGHSERRT
YYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAI
AAKLTKDAWNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGT
DVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPEFRDIIDATR
3D structure
PDB1qds The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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=0.048mM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qds, PDBe:1qds, PDBj:1qds
PDBsum1qds
PubMed10785370
UniProtP48499|TPIS_LEIME Triosephosphate isomerase

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