Structure of PDB 4k9d Chain E

Receptor sequence
>4k9dE (length=335) Species: 6279 (Brugia malayi) [Search protein sequence]
KPKVGINGFGRIGRLVLRAAVEKDTVDVVAVNDPFINIDYMVYMFKYDST
HGRFKGSVSAEGGKLIVTNTTHHISVHNSKDPAEIPWGVDGAEYVVESTG
VFTTTDKASAHLKGGAKKVIISAPSADAPMFVMGVNNDTYDKANNHIISN
ASCTTNCLAPLAKVIHDKFGIIEGLMTTVHATTATQKTVDGPSGKLWRDG
RGAGQNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPTPDVSVVDLTCRL
QKGATMDEIKAAVKEAANGPMKGILEYTEDQVVSTDFTGDTHSSIFDALA
CISLNPNFVKLIAWYDNEYGYSNRVVDLISYIASR
3D structure
PDB4k9d X-ray crystal structure of a Glyceraldehyde 3-phosphate dehydrogenase from Brugia malayi bound to the co-factor NAD
ChainE
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C157 H184
Catalytic site (residue number reindexed from 1) C153 H180
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 E N9 G12 R13 I14 D35 P36 F37 K84 T103 S126 C157 A188 N321 Y325 N7 G10 R11 I12 D33 P34 F35 K80 T99 S122 C153 A184 N317 Y321
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4k9d, PDBe:4k9d, PDBj:4k9d
PDBsum4k9d
PubMed
UniProtP48812|G3P_BRUMA Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=G3PD)

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