Structure of PDB 3qv1 Chain B

Receptor sequence
>3qv1B (length=336) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
KLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYDS
TLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGTG
VFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIISN
ASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRAR
AAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVS
KKTFAEEVNAAFRDSAEKELKGILDVCDEPLVSVDFRCSDFSTTIDSSLT
MVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK
3D structure
PDB3qv1 Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B G34 K38 Q39 R77 G37 K40 Q41 R80
BS02 NAD B G9 R10 I11 D32 T33 R77 G95 T96 G97 T119 C149 N313 Y317 G10 R11 I12 D35 T36 R80 G98 T99 G100 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

View graph for
Molecular Function
View graph for
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)

[Back to BioLiP]