1TVJ

Solution Structure of chick cofilin


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 20 
  • Selection Criteria: Structures with lowest energy, best covalent geometry, and least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

NMR Study of the Molecular Basis for Phosphoinositide Regulation of the Cofilin-Actin Interactions.

Gorbatyuk, V.Y.Nosworthy, N.J.Robson, S.A.Maciejewski, M.W.dos Remedios, C.G.King, G.F.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cofilin166Gallus gallusMutation(s): 0 
UniProt
Find proteins for P21566 (Gallus gallus)
Explore P21566 
Go to UniProtKB:  P21566
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP21566
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 20 
  • Selection Criteria: Structures with lowest energy, best covalent geometry, and least restraint violations 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-09-20
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Advisory, Database references, Derived calculations