Structure of PDB 6ghr Chain D Binding Site BS01

Receptor Information
>6ghr Chain D (length=338) Species: 197221 (Thermosynechococcus vestitus BP-1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SMVRVAINGFGRIGRNFMRCWLQRKANSKLEIVGINDTSDPRTNAHLLKY
DSMLGIFQDAEITADDDCIYAGGHAVKCVSDRNPENLPWSAWGIDLVIEA
TGVFTSREGASKHLSAGAKKVLITAPGKGNIPTYVVGVNHHTYDPSEDIV
SNASCTTNCLAPIVKVLHEAFGIQQGMMTTTHSYTGDQRLLDASHRDLRR
ARAAAMNIVPTSTGAAKAVGLVIPELQGKLNGIALRVPTPNVSVVDFVAQ
VEKPTIAEQVNQVIKEASETTMKGIIHYSELELVSSDYRGHNASSILDAS
LTMVLGGNLVKVVAWYDNEWGYSQRVLDLAEHMAAHWA
Ligand information
>6ghr Chain E (length=21) Species: 197221 (Thermosynechococcus vestitus BP-1) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
TSFQQYCDDNPDAAECRIYDD
Receptor-Ligand Complex Structure
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PDB6ghr Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria.
Resolution2.249 Å
Binding residue
(original residue number in PDB)
T37 S38 D39 S79 R81
Binding residue
(residue number reindexed from 1)
T38 S39 D40 S80 R82
Enzymatic activity
Catalytic site (original residue number in PDB) C154 H181
Catalytic site (residue number reindexed from 1) C155 H182
Enzyme Commision number 1.2.1.-
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
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:6ghr, PDBe:6ghr, PDBj:6ghr
PDBsum6ghr
PubMed31570616
UniProtQ8DIW5

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