1G1C

I1 DOMAIN FROM TITIN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.202 

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This is version 1.3 of the entry. See complete history. 


Literature

Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.

Mayans, O., Wuerges, J., Canela, S., Gautel, M., Wilmanns, M.

(2001) Structure 9: 331-340

  • DOI: https://doi.org/10.1016/s0969-2126(01)00591-3
  • Primary Citation of Related Structures:  
    1G1C

  • PubMed Abstract: 

    The giant muscle protein titin contributes to the filament system in skeletal and cardiac muscle cells by connecting the Z disk and the central M line of the sarcomere. One of the physiological functions of titin is to act as a passive spring in the sarcomere, which is achieved by the elastic properties of its central I band region. Titin contains about 300 domains of which more than half are folded as immunoglobulin-like (Ig) domains. Ig domain segments of the I band of titin have been extensively used as templates to investigate the molecular basis of protein elasticity.

    • Organizational Affiliation: 

    EMBL Hamburg Outstation, Germany.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
IMMUNOGLOBULIN-LIKE DOMAIN I1 FROM TITIN
A, B
99Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q8WZ42 (Homo sapiens)
Explore Q8WZ42 
Go to UniProtKB:  Q8WZ42
PHAROS:  Q8WZ42
GTEx:  ENSG00000155657 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8WZ42
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.202 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.3α = 90
b = 78.6β = 90
c = 79.6γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNSrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-10-12
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-12-11
    Changes: Advisory, Data collection, Database references, Derived calculations