Structure of PDB 1i32 Chain E

Receptor sequence
>1i32E (length=358) Species: 5665 (Leishmania mexicana) [Search protein sequence]
APIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVVDMSTNAEYFAYQM
KHDTVHGRPKYTVEAVKSSPSVETADVLVVNGHRIKCVKAQRNPADLPWG
KLGVDYVIESTGLFTDKLKAEGHIKGGAKKVVISAPASGGAKTIVMGVNQ
HEYSPASHHVVSNASCTTNCLAPIVHVLTKENFGIETGLMTTIHSYTATQ
KTVDGVSLKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRV
PTPDVSVVDLTFRATRDTSIQEIDKAIKKAAQTYMKGILGFTDEELVSAD
FINDNRSSVYDSKATLQNNLPGEKRFFKVVSWYDNEWAYSHRVVDLVRYM
AAKDAASS
3D structure
PDB1i32 Conformational changes in Leishmania mexicana glyceraldehyde-3-phosphate dehydrogenase induced by designed inhibitors.
ChainE
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C166 H194
Catalytic site (residue number reindexed from 1) C166 H194
Enzyme Commision number 1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating).
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 NMD E G9 G11 D38 M39 S40 A90 Q91 R92 T111 L113 G9 G11 D38 M39 S40 A90 Q91 R92 T111 L113
Gene Ontology
Molecular Function
GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006096 glycolytic process
Cellular Component
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:1i32, PDBe:1i32, PDBj:1i32
PDBsum1i32
PubMed11371162
UniProtQ27890|G3PG_LEIME Glyceraldehyde-3-phosphate dehydrogenase, glycosomal (Gene Name=GAPG)

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