Structure of PDB 3qv1 Chain D Binding Site BS01
Receptor Information
>3qv1 Chain D (length=337) Species:
3702
(Arabidopsis thaliana) [
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AKLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYD
STLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGT
GVFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIIS
NASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRA
RAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQV
SKKTFAEEVNAAFRDSAEKELKGILDVCDEPLVSVDFRCSDFSTTIDSSL
TMVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK
Ligand information
>3qv1 Chain G (length=21) Species:
3702
(Arabidopsis thaliana) [
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DPLEEYCKDNPETNECRTYDN
Receptor-Ligand Complex Structure
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PDB
3qv1
Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
R77 V98 C149 T150 H176 G180 D181 R183 S188 H190 R191 R195 T208 G209 R231
Binding residue
(residue number reindexed from 1)
R81 V102 C154 T155 H181 G185 D186 R188 S193 H194 R195 R199 T212 G213 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
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Molecular Function
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Biological 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)
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