1QLS

S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN I N-TERMINUS

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.214 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Structural Basis of the Ca2+ Dependent Association between S100C (S100A11) and its Target, the N-Terminal Part of Annexin I

Rety, S., Osterloh, D., Arie, J.P., Tabaries, S., Seeman, J., Russo-Marie, F., Gerke, V., Lewit-Bentley, A.

(2000) Structure 8: 175

  • DOI: https://doi.org/10.1016/s0969-2126(00)00093-9
  • Primary Citation of Related Structures:  
    1QLS

  • PubMed Abstract: 

    S100C (S100A11) is a member of the S100 calcium-binding protein family, the function of which is not yet entirely clear, but may include cytoskeleton assembly and dynamics. S100 proteins consist of two EF-hand calcium-binding motifs, connected by a flexible loop. Like several other members of the family, S100C forms a homodimer. A number of S100 proteins form complexes with annexins, another family of calcium-binding proteins that also bind to phospholipids. Structural studies have been undertaken to understand the basis of these interactions.

    • Organizational Affiliation: 

    Centre Universitaire Paris-Sud, LURE (CNRS, CEA, MENRT), Orsay, 91898, France.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
S100C PROTEIN99Sus scrofaMutation(s): 0 
UniProt
Find proteins for P31950 (Sus scrofa)
Explore P31950 
Go to UniProtKB:  P31950
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP31950
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ANNEXIN IB [auth D]12Homo sapiensMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for P04083 (Homo sapiens)
Explore P04083 
Go to UniProtKB:  P04083
PHAROS:  P04083
GTEx:  ENSG00000135046 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04083
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.214 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.51α = 90
b = 77.51β = 90
c = 111.61γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-02-25
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-03-06
    Changes: Data collection, Derived calculations, Experimental preparation, Other
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description