Structure of PDB 2b4t Chain Q

Receptor sequence
>2b4tQ (length=333) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
TKLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVH
GQFPCEVTHADGFLLIGEKKVSVFAEKDPSQIPWGKCQVDVVCESTGVFL
TKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASC
TTNCLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKGGKDWRAGR
CALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIGTVSVVDLVCRLQ
KPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAG
LALNDNFFKLVSWYDNEWGYSNRVLDLAVHITT
3D structure
PDB2b4t Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 A resolution reveals intriguing extra electron density in the active site
ChainQ
Resolution2.5 Å
3D
structure
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Enzymatic activity
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 Q G10 G12 R13 I14 D35 P36 F37 T99 S122 C153 A184 N319 Y323 G7 G9 R10 I11 D32 P33 F34 T96 S119 C150 A181 N316 Y320
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
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2b4t, PDBe:2b4t, PDBj:2b4t
PDBsum2b4t
PubMed16345073
UniProtQ8T6B1

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