Structure of PDB 3rvd Chain Q

Receptor sequence
>3rvdQ (length=336) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
KLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYDS
TLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGTG
VFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIISN
ASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRAR
AAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVS
KKTFAEEVNAAFRDSAEKELKGILDVCDEPLVSVDFRCSDFSTTIDSSLT
MVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK
3D structure
PDB3rvd Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.
ChainQ
Resolution2.7 Å
3D
structure
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Enzymatic activity
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 Q R77 V98 R183 S188 H190 R191 R80 V101 R187 S192 H193 R194
BS02 NAD Q F8 G9 R10 I11 D32 T33 R77 G95 T96 G97 F99 T119 C149 N313 Y317 F9 G10 R11 I12 D35 T36 R80 G98 T99 G100 F102 T122 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:3rvd, PDBe:3rvd, PDBj:3rvd
PDBsum3rvd
PubMed22514274
UniProtP25856|G3PA1_ARATH Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic (Gene Name=GAPA1)

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