Structure of PDB 2vyv Chain D

Receptor sequence

>2vyvD (length=334) Species: 10116 (Rattus norvegicus)

MVKVGINGFGRIGRLVLRVCMEKGVRVVAVNDPFIDPEYMVYMFKYDSTH
GRYKGTVEHKNGRLVVDNLEINVFQCKEPKEIPWSSVGNPYVVEATGVYL
SIEAASGHISSGARRVIVTAPSPDAPMLVMGVNEKDYNPGSMTVVSNASC
TTNCLAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGA
HQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLAQP
ASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIA
LNDNFVKLVSWYDNEYGYSHRVVDLLRYMFSREK

3D structure

• PDB: 2vyv Structure of Insoluble Rat Sperm Glyceraldehyde-3-Phosphate Dehydrogenase (Gapdh) Via Heterotetramer Formation with Escherichia Coli Gapdh Reveals Target for Contraceptive Design.
• Chain: D
• Resolution: 2.38 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C149 H176
• Catalytic site (residue number reindexed from 1): C150 H177
• 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	1GP	D	A149 H176 T179 T181 R231	A150 H177 T180 T182 R232
BS02	NAD	D	N6 G7 G9 R10 I11 D31 P32 F33 T95 G96 T118 A149 N313 Y317	N7 G8 G10 R11 I12 D32 P33 F34 T96 G97 T119 A150 N314 Y318

Gene Ontology

Molecular Function

• 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

External links

• PDB: RCSB:2vyv, PDBe:2vyv, PDBj:2vyv
• PDBsum: 2vyv
• PubMed: 19542219
• UniProt: Q9ESV6|G3PT_RAT Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gene Name=Gapdhs)