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PDBsum entry 3ogc

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protein metals Protein-protein interface(s) links
Membrane protein PDB id
3ogc

 

 

 

 

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Contents
Protein chains
219 a.a.
212 a.a.
103 a.a.
Metals
_NA ×2
PDB id:
3ogc
Name: Membrane protein
Title: Kcsa e71a variant in presence of na+
Structure: Antibody fab fragment heavy chain. Chain: a. Engineered: yes. Antibody fab fragment light chain. Chain: b. Engineered: yes. Voltage-gated potassium channel. Chain: c. Fragment: unp residues 2-124.
Source: Mus musculus. Mouse. Organism_taxid: 10090. Streptomyces lividans. Organism_taxid: 1916. Gene: kcsa, skc1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
3.80Å     R-factor:   0.249     R-free:   0.283
Authors: J.G.Mccoy,C.M.Nimigean
Key ref: W.W.Cheng et al. (2011). Mechanism for selectivity-inactivation coupling in KcsA potassium channels. Proc Natl Acad Sci U S A, 108, 5272-5277. PubMed id: 21402935
Date:
16-Aug-10     Release date:   16-Mar-11    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 219 a.a.
Protein chain
No UniProt id for this chain
Struc: 212 a.a.
Protein chain
Pfam   ArchSchema ?
P0A334  (KCSA_STRLI) -  pH-gated potassium channel KcsA from Streptomyces lividans
Seq:
Struc:
160 a.a.
103 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
Proc Natl Acad Sci U S A 108:5272-5277 (2011)
PubMed id: 21402935  
 
 
Mechanism for selectivity-inactivation coupling in KcsA potassium channels.
W.W.Cheng, J.G.McCoy, A.N.Thompson, C.G.Nichols, C.M.Nimigean.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21518829 C.M.Nimigean, and T.W.Allen (2011).
Origins of ion selectivity in potassium channels from the perspective of channel block.
  J Gen Physiol, 137, 405-413.  
  21518831 P.D.Dixit, and D.Asthagiri (2011).
Thermodynamics of ion selectivity in the KcsA K+ channel.
  J Gen Physiol, 137, 427-433.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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