Structure of PDB 3k2b Chain D

Receptor sequence
>3k2bD (length=336) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
KLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYDS
TLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGTG
VFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIISN
ASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRAR
AAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVS
KKTFAEEVNAAFRDSAEKELKGILDVCDEPLVSVDFRCSDFSTTIDSSLT
MVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK
3D structure
PDB3k2b Structure of photosynthetic glyceraldehyde-3-phosphate dehydrogenase (isoform A4) from Arabidopsis thaliana in complex with NAD
ChainD
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 D F8 G9 R10 I11 D32 T33 R77 T96 G97 T119 A120 C149 N313 Y317 F9 G10 R11 I12 D35 T36 R80 T99 G100 T122 A123 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:3k2b, PDBe:3k2b, PDBj:3k2b
PDBsum3k2b
PubMed20516587
UniProtP25856|G3PA1_ARATH Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic (Gene Name=GAPA1)

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