Structure of PDB 4k9d Chain B

Receptor sequence

>4k9dB (length=338) Species: 6279 (Brugia malayi)

SKPKVGINGFGRIGRLVLRAAVEKDTVDVVAVNDPFINIDYMVYMFKYDS
THGRFKGSVSAEGGKLIVTNGKTTHHISVHNSKDPAEIPWGVDGAEYVVE
STGVFTTTDKASAHLKGGAKKVIISAPSADAPMFVMGVNNDTYDKANNHI
ISNASCTTNCLAPLAKVIHDKFGIIEGLMTTVHATTATQKTVDGPSGKLW
RDGRGAGQNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPTPDVSVVDLT
CRLQKGATMDEIKAAVKEAANGPMKGILEYTEDQVVSTDFTGDTHSSIFD
ALACISLNPNFVKLIAWYDNEYGYSNRVVDLISYIASR

3D structure

• PDB: 4k9d X-ray crystal structure of a Glyceraldehyde 3-phosphate dehydrogenase from Brugia malayi bound to the co-factor NAD
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C157 H184
• Catalytic site (residue number reindexed from 1): C156 H183
• 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	B	G10 G12 R13 I14 D35 P36 F37 T103 G104 S126 C157 N321 Y325	G9 G11 R12 I13 D34 P35 F36 T102 G103 S125 C156 N320 Y324

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:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:4k9d, PDBe:4k9d, PDBj:4k9d
• PDBsum: 4k9d
• UniProt: P48812|G3P_BRUMA Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=G3PD)