Structure of PDB 3rvd Chain O Binding Site BS01

Receptor Information

>3rvd Chain O (length=337) Species: 3702 (Arabidopsis thaliana)

AKLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYD
STLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGT
GVFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIIS
NASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRA
RAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQV
SKKTFAEEVNAAFRDSAEKELKGILDVCDEPLVSVDFRCSDFSTTIDSSL
TMVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK

Ligand information

>3rvd Chain K (length=21) Species: 3702 (Arabidopsis thaliana)

DPLEEYCKDNPETNECRTYDN

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3rvd Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.
• Resolution: 2.7 Å
• Binding residue (original residue number in PDB): R77 V98 S148 T150 H176 G180 D181 R183 S188 H190 R191 R195 T208 A210 R231
• Binding residue (residue number reindexed from 1): R81 V102 S153 T155 H181 G185 D186 R188 S193 H194 R195 R199 T212 A214 R235

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).

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