Structure of PDB 3sth Chain A

Receptor sequence
>3sthA (length=339) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
MVCKLGINGFGRIGRLVFRAAMERGDVEVLAINDPFMSLDYMVYLLRYDS
VHGHYPGEVSHKDGKLIVGGKAVTVFNEKEPTAIPWGQAGVHYICESTGI
FLTKEKAQAHLTNGAKKVIMSAPPKDDTPMFVMGVNNDQYKSSDVIVSNA
SCTTNCLAPLAKIVHDKFGIVEGLMTTVHAMTANQLTVDGPSKGGKDWRA
GRSAGVNIIPASTGAAKAVGKIIPSLNGKLTGMAFRVPVPDVSVVDLTCK
LAKPAKYEDIVAAVKEAATSGPMKGIISYTDEEVVSSDFVHCKFSSVFDI
NAGIMLNDTFVKLVSWYDNEWGYSNRLVELAHYMSVQDG
3D structure
PDB3sth Membrane skeletal association and post-translational allosteric regulation of Toxoplasma gondii GAPDH1.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C152 H179
Catalytic site (residue number reindexed from 1) C152 H179
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 N8 G9 G11 R12 I13 D34 P35 F36 S97 T98 G99 S121 C152 A183 N319 Y323 N8 G9 G11 R12 I13 D34 P35 F36 S97 T98 G99 S121 C152 A183 N319 Y323
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:3sth, PDBe:3sth, PDBj:3sth
PDBsum3sth
PubMed27859784
UniProtQ9BKE2

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