Structure of PDB 3hja Chain D

Receptor sequence
>3hjaD (length=334) Species: 224326 (Borreliella burgdorferi B31) [Search protein sequence]
MKLAINGFGRIGRNVFKIAFERGIDIVAINDLTDPKTLAHLLKYDSTFGV
YNKKVESRDGAIVVDGREIKIIAERDPKNLPWAKLGIDVVIESTGVFSSA
TSDKGGYLDHVNHAGAKKVILTVPAKDEIKTIVLGVNDHDINSDLKAVSN
ASCTTNCLAPLAKVLHESFGIEQGLMTTVHAYTNDQRILDLPHSDLRRAR
AAALSIIPTSTGAAKAVGLVLPELKGKLNGTSMRVPVPTGSIVDLTVQLK
KKDVTKEEINSVLRKASETPELKGILGYTEDPIVSSDIKGNSHSSIVDGL
ETMVLENGFAKILSWYDNEFGYSTRVVDLAQKLV
3D structure
PDB3hja Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Borrelia burgdorferi
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C153 H180
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 D G9 R10 I11 D31 L32 T94 G95 F97 T122 V123 C153 N184 N318 Y322 G9 R10 I11 D31 L32 T94 G95 F97 T122 V123 C153 N184 N318 Y322
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: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:3hja, PDBe:3hja, PDBj:3hja
PDBsum3hja
PubMed
UniProtP46795|G3P_BORBU Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=gap)

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