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PDBsum entry 5k2c

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protein ligands metals links
Membrane protein PDB id
5k2c

 

 

 

 

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Contents
Protein chain
396 a.a.
Ligands
ZMA
CLR ×3
OLC ×10
OLA ×11
PEG
Metals
_NA
Waters ×106
PDB id:
5k2c
Name: Membrane protein
Title: 1.9 angstrom a2a adenosine receptor structure with sulfur sad phasing and phase extension using xfel data
Structure: Adenosine receptor a2a/soluble cytochrome b562 chimera. Chain: a. Synonym: cytochrome b-562. Engineered: yes
Source: Homo sapiens, escherichia coli. Human. Organism_taxid: 9606, 562. Gene: adora2a, adora2, cybc. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108
Resolution:
1.90Å     R-factor:   0.174     R-free:   0.208
Authors: A.Batyuk,L.Galli,A.Ishchenko,G.W.Han,C.Gati,P.Popov,M.-Y.Lee, B.Stauch,T.A.White,A.Barty,A.Aquila,M.S.Hunter,M.Liang,S.Boutet, M.Pu,Z.-J.Liu,G.Nelson,D.James,C.Li,Y.Zhao,J.C.H.Spence,W.Liu, P.Fromme,V.Katritch,U.Weierstall,R.C.Stevens,V.Cherezov,Gpcr Network (Gpcr)
Key ref: A.Batyuk et al. (2016). Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. Sci Adv, 2, e1600292. PubMed id: 27679816 DOI: 10.1126/sciadv.1600292
Date:
18-May-16     Release date:   21-Sep-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0ABE7  (C562_ECOLX) -  Soluble cytochrome b562 from Escherichia coli
Seq:
Struc:
128 a.a.
396 a.a.*
Protein chain
Pfam   ArchSchema ?
P29274  (AA2AR_HUMAN) -  Adenosine receptor A2a from Homo sapiens
Seq:
Struc:
412 a.a.
396 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 112 residue positions (black crosses)

 

 
DOI no: 10.1126/sciadv.1600292 Sci Adv 2:e1600292 (2016)
PubMed id: 27679816  
 
 
Native phasing of x-ray free-electron laser data for a G protein-coupled receptor.
A.Batyuk, L.Galli, A.Ishchenko, G.W.Han, C.Gati, P.A.Popov, M.Y.Lee, B.Stauch, T.A.White, A.Barty, A.Aquila, M.S.Hunter, M.Liang, S.Boutet, M.Pu, Z.J.Liu, G.Nelson, D.James, C.Li, Y.Zhao, J.C.Spence, W.Liu, P.Fromme, V.Katritch, U.Weierstall, R.C.Stevens, V.Cherezov.
 
  ABSTRACT  
 
No abstract given.

 

 

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