Structure of PDB 2pkr Chain I

Receptor sequence
>2pkrI (length=337) Species: 3562 (Spinacia oleracea) [Search protein sequence]
KLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVINDTGGVKQASHLLKYDS
ILGTFDADVKTAGDSAISVDGKVIKVVSDRNPVNLPWGDMGIDLVIEGTG
VFVDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNEEGYTHADTIISN
ASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRAR
AACLNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVS
KKTFAEEVNAAFRESADNELKGILSVCDEPLVSIDFRCTDVSSTIDSSLT
MVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANKWQG
3D structure
PDB2pkr Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-glyceraldehyde-3-phosphate dehydrogenase.
ChainI
Resolution2.4 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 NDP I G9 R10 I11 R77 G95 T96 G97 F99 T119 A120 N313 Y317 G10 R11 I12 R80 G98 T99 G100 F102 T122 A123 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:2pkr, PDBe:2pkr, PDBj:2pkr
PDBsum2pkr
PubMed17573533
UniProtP19866|G3PA_SPIOL Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic (Gene Name=GAPA)

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