Structure of PDB 1jn0 Chain A

Receptor sequence
>1jn0A (length=334) Species: 3562 (Spinacia oleracea) [Search protein sequence]
KLKVAINGFGRIGRNFLRCWHGKDSPLDVVVINDTGGVKQASHLLKYDSI
LGTFDADVKTAGDSAISVGKVIKVVSDRNPVNLPWGDMGIDLVIEGTGVF
VDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNEEGYTHADTIISNAS
CTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAA
CLNIVPTSTGAAKAVALVLPQLKGKLNGIALRVPTPNVSVVDLVVQVSKK
TFAEEVNAAFRESADQELKGILSVCDEPLVSIDFRCTDVSSTIDSSLTMV
MGDDMVKVIAWYDNEWGYSQRVVDLADIVANKWQ
3D structure
PDB1jn0 Crystal structure of the non-regulatory A(4 )isoform of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase complexed with NADP.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C149 H176
Catalytic site (residue number reindexed from 1) C151 H178
Enzyme Commision number 1.2.1.13: glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (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 NDP A G9 R10 I11 N31 T33 R77 T96 G97 T119 C149 N313 Y317 G10 R11 I12 N33 T35 R78 T97 G98 T120 C151 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1jn0, PDBe:1jn0, PDBj:1jn0
PDBsum1jn0
PubMed11846565
UniProtP19866|G3PA_SPIOL Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic (Gene Name=GAPA)

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