Structure of PDB 3qv1 Chain D

Receptor sequence

>3qv1D (length=337) Species: 3702 (Arabidopsis thaliana)

AKLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYD
STLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGT
GVFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIIS
NASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRA
RAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQV
SKKTFAEEVNAAFRDSAEKELKGILDVCDEPLVSVDFRCSDFSTTIDSSL
TMVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK

3D structure

• PDB: 3qv1 Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.
• Chain: D
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C149 H176
• Catalytic site (residue number reindexed from 1): C154 H181
• 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	peptide	D	R77 V98 C149 T150 H176 G180 D181 R183 S188 H190 R191 R195 T208 G209 R231	R81 V102 C154 T155 H181 G185 D186 R188 S193 H194 R195 R199 T212 G213 R235
BS02	NAD	D	G9 R10 I11 D32 R77 G95 T96 G97 T119 C149 N313 Y317	G11 R12 I13 D36 R81 G99 T100 G101 T123 C154 N317 Y321

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

External links

• PDB: RCSB:3qv1, PDBe:3qv1, PDBj:3qv1
• PDBsum: 3qv1
• PubMed: 22514274
• UniProt: P25856|G3PA1_ARATH Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic (Gene Name=GAPA1)