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PDBsum entry 4j4q

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protein ligands Protein-protein interface(s) links
Signaling protein PDB id
4j4q

 

 

 

 

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Contents
Protein chains
326 a.a.
11 a.a.
Ligands
NAG-NAG-BMA-MAN
GLC-GLC
BOG ×4
PLM
SO4 ×2
ACT
Waters ×32
PDB id:
4j4q
Name: Signaling protein
Title: Crystal structure of active conformation of gpcr opsin stabilized by octylglucoside
Structure: Rhodopsin. Chain: a. Guanine nucleotide-binding protein g(t) subunit alpha-1. Chain: b. Fragment: c-terminal derived peptide, unp residues 340-350. Synonym: transducin alpha-1 chain. Engineered: yes. Mutation: yes
Source: Bos taurus. Bovine. Organism_taxid: 9913. Strain: bovine. Synthetic: yes. Other_details: this peptide was chemically synthesized with k341l and c347v mutation
Resolution:
2.65Å     R-factor:   0.218     R-free:   0.230
Authors: J.H.Park,T.Morizumi,Y.Li,J.E.Hong,E.F.Pai,K.P.Hofmann,H.W.Choe, O.P.Ernst
Key ref: J.H.Park et al. (2013). Opsin, a structural model for olfactory receptors? Angew Chem Int Ed Engl, 52, 11021-11024. PubMed id: 24038729 DOI: 10.1002/anie.201302374
Date:
07-Feb-13     Release date:   30-Oct-13    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02699  (OPSD_BOVIN) -  Rhodopsin from Bos taurus
Seq:
Struc:
348 a.a.
326 a.a.
Protein chain
Pfam   ArchSchema ?
P04695  (GNAT1_BOVIN) -  Guanine nucleotide-binding protein G(t) subunit alpha-1 from Bos taurus
Seq:
Struc:
350 a.a.
11 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1002/anie.201302374 Angew Chem Int Ed Engl 52:11021-11024 (2013)
PubMed id: 24038729  
 
 
Opsin, a structural model for olfactory receptors?
J.H.Park, T.Morizumi, Y.Li, J.E.Hong, E.F.Pai, K.P.Hofmann, H.W.Choe, O.P.Ernst.
 
  ABSTRACT  
 
Receptor-ligand interaction: Olfactory receptors (ORs) are G-protein-coupled receptors (GPCRs), which detect signaling molecules such as hormones and odorants. The structure of opsin, the GPCR employed in vision, with a detergent molecule bound deep in its orthosteric ligand-binding pocket provides a template for OR homology modeling, thus enabling investigation of the structural basis of the mechanism of odorant-receptor recognition.
 

 

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