Structure of PDB 1nbo Chain A

Receptor sequence
>1nboA (length=337) Species: 3562 (Spinacia oleracea) [Search protein sequence]
KLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVINDTGGVKQASHLLKYDS
ILGTFDADVKTAGDSAISVDGKVIKVVSDRNPVNLPWGDMGIDLVIEGTG
VFVDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNEEGYTHADTIISN
ASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRAR
AACLNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVS
KKTFAEEVNAAFRESADNELKGILSVCDEPLVSIDFRCTDVSSTIDSSLT
MVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANKWQA
3D structure
PDB1nbo Dual Coenzyme Specificity of Photosynthetic Glyceraldehyde-3-phosphate Dehydrogenase Interpreted by the Crystal Structure of A(4) Isoform Complexed with NAD
ChainA
Resolution2.6 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) C153 H180
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 NAD A G9 R10 I11 D32 R77 T96 G97 F99 T119 A120 C149 N313 E314 Y317 G10 R11 I12 D35 R80 T99 G100 F102 T122 A123 C153 N316 E317 Y320
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:1nbo, PDBe:1nbo, PDBj:1nbo
PDBsum1nbo
PubMed12705826
UniProtP19866|G3PA_SPIOL Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic (Gene Name=GAPA)

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