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PDBsum entry 4dck

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protein metals Protein-protein interface(s) links
Transport protein/signaling protein PDB id
4dck

 

 

 

 

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Contents
Protein chains
153 a.a.
134 a.a.
148 a.a.
Metals
_MG ×3
Waters ×202
PDB id:
4dck
Name: Transport protein/signaling protein
Title: Crystal structure of thE C-terminus of voltage-gated sodium channel in complex with fgf13 and cam
Structure: Sodium channel protein type 5 subunit alpha. Chain: a. Fragment: c-terminal domain of nav1.5. Synonym: hh1, sodium channel protein cardiac muscle subunit alpha, sodium channel protein type v subunit alpha, voltage-gated sodium channel subunit alpha nav1.5. Engineered: yes. Calmodulin. Chain: b.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: scn5a. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: calm1, calm, cam, cam1, calm2, cam2, camb, calm3, calml2, cam3, camc, camiii. Gene: fgf13, fhf2.
Resolution:
2.20Å     R-factor:   0.211     R-free:   0.227
Authors: B.C.Chung,C.Wang,H.Yan,G.S.Pitt,S.Y.Lee
Key ref: C.Wang et al. (2012). Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure, 20, 1167-1176. PubMed id: 22705208
Date:
17-Jan-12     Release date:   27-Jun-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q14524  (SCN5A_HUMAN) -  Sodium channel protein type 5 subunit alpha from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2016 a.a.
153 a.a.
Protein chain
Pfam   ArchSchema ?
P0DP23  (CALM1_HUMAN) -  Calmodulin-1 from Homo sapiens
Seq:
Struc:
149 a.a.
134 a.a.
Protein chain
Pfam   ArchSchema ?
Q92913  (FGF13_HUMAN) -  Fibroblast growth factor 13 from Homo sapiens
Seq:
Struc:
245 a.a.
148 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Structure 20:1167-1176 (2012)
PubMed id: 22705208  
 
 
Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin.
C.Wang, B.C.Chung, H.Yan, S.Y.Lee, G.S.Pitt.
 
  ABSTRACT  
 
No abstract given.

 

 

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