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PDBsum entry 4dx5

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protein ligands Protein-protein interface(s) links
Membrane protein, transport protein PDB id
4dx5

 

 

 

 

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Contents
Protein chains
1044 a.a.
156 a.a.
Ligands
GOL ×15
LMT ×8
OCT ×7
D10 ×6
HEX ×5
D12 ×4
MIY
C14
LMU
DD9
SO4
UND
Waters ×1783
PDB id:
4dx5
Name: Membrane protein, transport protein
Title: Transport of drugs by the multidrug transporter acrb involves an access and a deep binding pocket that are separated by a switch-loop
Structure: Acriflavine resistance protein b. Chain: a, b, c. Engineered: yes. Darpin. Chain: d, e. Engineered: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: acrb, acre, b0462, jw0451. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic construct. Artificial gene. Organism_taxid: 32630.
Resolution:
1.90Å     R-factor:   0.202     R-free:   0.231
Authors: T.Eicher,H.Cha,M.A.Seeger,L.Brandstaetter,J.El-Delik,J.A.Bohnert, W.V.Kern,F.Verrey,M.G.Gruetter,K.Diederichs,K.M.Pos
Key ref: T.Eicher et al. (2012). Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop. Proc Natl Acad Sci U S A, 109, 5687-5692. PubMed id: 22451937
Date:
27-Feb-12     Release date:   02-May-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P31224  (ACRB_ECOLI) -  Multidrug efflux pump subunit AcrB from Escherichia coli (strain K12)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1049 a.a.
1044 a.a.
Protein chains
No UniProt id for this chain
Struc: 156 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Proc Natl Acad Sci U S A 109:5687-5692 (2012)
PubMed id: 22451937  
 
 
Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop.
T.Eicher, H.J.Cha, M.A.Seeger, L.Brandstätter, J.El-Delik, J.A.Bohnert, W.V.Kern, F.Verrey, M.G.Grütter, K.Diederichs, K.M.Pos.
 
  ABSTRACT  
 
No abstract given.

 

 

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