Structure of PDB 1nbo Chain B

Receptor sequence
>1nboB (length=336) Species: 3562 (Spinacia oleracea) [Search protein sequence]
KLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVINDTGGVKQASHLLKYDS
ILGTFDADVKTAGDSAISVDGKVIKVVSDRNPVNLPWGDMGIDLVIEGTG
VFVDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNEEGYTHADTIISN
ASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRAR
AACLNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVS
KKTFAEEVNAAFRESADNELKGILSVCDEPLVSIDFRCTDVSSTIDSSLT
MVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANKWQ
3D structure
PDB1nbo Dual Coenzyme Specificity of Photosynthetic Glyceraldehyde-3-phosphate Dehydrogenase Interpreted by the Crystal Structure of A(4) Isoform Complexed with NAD
ChainB
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 B G9 R10 I11 D32 T33 R77 T96 G97 F99 T119 C149 N313 Y317 G10 R11 I12 D35 T36 R80 T99 G100 F102 T122 C153 N316 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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