Structure of PDB 4lsm Chain A

Receptor sequence
>4lsmA (length=331) Species: 353153 (Trypanosoma cruzi strain CL Brener) [Search protein sequence]
TIKIGINGFGRIGRMVFRAAQHRNDIEIVGINDLLDADYMAYMLKYDSTH
GRYGGMVEVREGALVVNGKKIRVTSERDPANLKWNEVGAVVVVESTGLFL
TDETARKHIQAGAKKVVMTGPPKDDTPMFVMGVNNTMYKGQEIVSNASCT
TNCLAPLAKIIHEKFGIVEGLMTTVHATTATQKTVDGPSQKDWRGGRGAA
QNIIPSATGAAKAVGKVIPALNGRLTGMAFRVPTPNVSVVDLTARLERPA
TYEQICAAIKAASEGELKGILGYTEDEVVSTDMNGVALTSVFDVKAGISL
NDRFVKLISWYDNETGYSHKVLDLVAYISAH
3D structure
PDB4lsm Crystal structure of a glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C156 H183
Catalytic site (residue number reindexed from 1) C149 H176
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 NAD A G17 R18 I19 D40 T103 G104 T126 C156 A187 N320 Y324 G10 R11 I12 D33 T96 G97 T119 C149 A180 N313 Y317
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4lsm, PDBe:4lsm, PDBj:4lsm
PDBsum4lsm
PubMed
UniProtQ4DZT1

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