Structure of PDB 3qv1 Chain F Binding Site BS01

Receptor Information
>3qv1 Chain F (length=336) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYDS
TLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGTG
VFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIISN
ASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRAR
AAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVS
KKTFAEEVNAAFRDSAEKELKGILDVCDEPLVSVDFRCSDFSTTIDSSLT
MVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK
Ligand information
>3qv1 Chain I (length=19) Species: 3702 (Arabidopsis thaliana) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
DPLEEYCKDNPETNECRTY
Receptor-Ligand Complex Structure
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PDB3qv1 Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.
Resolution2.0 Å
Binding residue
(original residue number in PDB)
V98 G180 D181 R183 S188 H190 R191 R195
Binding residue
(residue number reindexed from 1)
V101 G184 D185 R187 S192 H193 R194 R198
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).
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:3qv1, PDBe:3qv1, PDBj:3qv1
PDBsum3qv1
PubMed22514274
UniProtP25856|G3PA1_ARATH Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic (Gene Name=GAPA1)

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