Structure of PDB 3rvd Chain D

Receptor sequence
>3rvdD (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.
ChainD
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
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 S148 C149 T150 H176 G180 D181 R183 S188 H190 R191 R195 G209 R231 R80 V101 S152 C153 T154 H180 G184 D185 R187 S192 H193 R194 R198 G212 R234
BS02 NAD D G9 R10 I11 N31 D32 T33 R77 T119 C149 N313 Y317 G10 R11 I12 N34 D35 T36 R80 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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