Structure of PDB 6ghr Chain A Binding Site BS01
Receptor Information
>6ghr Chain A (length=338) Species:
197221
(Thermosynechococcus vestitus BP-1) [
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SMVRVAINGFGRIGRNFMRCWLQRKANSKLEIVGINDTSDPRTNAHLLKY
DSMLGIFQDAEITADDDCIYAGGHAVKCVSDRNPENLPWSAWGIDLVIEA
TGVFTSREGASKHLSAGAKKVLITAPGKGNIPTYVVGVNHHTYDPSEDIV
SNASCTTNCLAPIVKVLHEAFGIQQGMMTTTHSYTGDQRLLDASHRDLRR
ARAAAMNIVPTSTGAAKAVGLVIPELQGKLNGIALRVPTPNVSVVDFVAQ
VEKPTIAEQVNQVIKEASETTMKGIIHYSELELVSSDYRGHNASSILDAS
LTMVLGGNLVKVVAWYDNEWGYSQRVLDLAEHMAAHWA
Ligand information
>6ghr Chain E (length=21) Species:
197221
(Thermosynechococcus vestitus BP-1) [
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TSFQQYCDDNPDAAECRIYDD
Receptor-Ligand Complex Structure
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PDB
6ghr
Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria.
Resolution
2.249 Å
Binding residue
(original residue number in PDB)
R81 V102 T155 H181 T184 G185 D186 R188 S193 H194 R195 R199 T212 G213 R235
Binding residue
(residue number reindexed from 1)
R82 V103 T156 H182 T185 G186 D187 R189 S194 H195 R196 R200 T213 G214 R236
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
PDBsum
6ghr
PubMed
31570616
UniProt
Q8DIW5
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