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PDBsum entry 3v3y

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protein ligands metals Protein-protein interface(s) links
Electron transport PDB id
3v3y

 

 

 

 

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Contents
Protein chains
241 a.a.
281 a.a.
302 a.a.
Ligands
LDA ×8
BCL ×4
BPH ×2
U10 ×2
DIO ×3
SPN
PO4 ×3
Metals
_CL
_FE
Waters ×92
PDB id:
3v3y
Name: Electron transport
Title: Photosynthetic reaction center from rhodobacter sphaeroides strain rv
Structure: Reaction center protein h chain. Chain: h. Synonym: photosynthetic reaction center h subunit. Engineered: yes. Reaction center protein l chain. Chain: l. Synonym: photosynthetic reaction center l subunit. Engineered: yes. Reaction center protein m chain.
Source: Rhodobacter sphaeroides. Organism_taxid: 1063. Gene: puha. Expressed in: rhodobacter sphaeroides. Expression_system_taxid: 1063. Gene: pufl. Gene: pufm.
Resolution:
2.80Å     R-factor:   0.246     R-free:   0.284
Authors: A.G.Gabdulkhakov,T.Y.Fufina,L.G.Vasilieva,V.A.Shuvalov
Key ref: L.G.Vasilieva et al. (2012). The site-directed mutation I(L177)H in Rhodobacter sphaeroides reaction center affects coordination of P(A) and B(B) bacteriochlorophylls. Biochim Biophys Acta, 1817, 1407-1417. PubMed id: 22365928
Date:
14-Dec-11     Release date:   14-Mar-12    
PROCHECK
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 Headers
 References

Protein chain
P0C0Y7  (RCEH_CERSP) -  Reaction center protein H chain from Cereibacter sphaeroides
Seq:
Struc:
260 a.a.
241 a.a.
Protein chain
P0C0Y8  (RCEL_CERSP) -  Reaction center protein L chain from Cereibacter sphaeroides
Seq:
Struc:
282 a.a.
281 a.a.*
Protein chain
P0C0Y9  (RCEM_CERSP) -  Reaction center protein M chain from Cereibacter sphaeroides
Seq:
Struc:
308 a.a.
302 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
Biochim Biophys Acta 1817:1407-1417 (2012)
PubMed id: 22365928  
 
 
The site-directed mutation I(L177)H in Rhodobacter sphaeroides reaction center affects coordination of P(A) and B(B) bacteriochlorophylls.
L.G.Vasilieva, T.Y.Fufina, A.G.Gabdulkhakov, M.M.Leonova, R.A.Khatypov, V.A.Shuvalov.
 
  ABSTRACT  
 
No abstract given.

 

 

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