1B8R

PARVALBUMIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.177 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin.

Cates, M.S.Berry, M.B.Ho, E.L.Li, Q.Potter, J.D.Phillips Jr., G.N.

(1999) Structure 7: 1269-1278

  • DOI: https://doi.org/10.1016/s0969-2126(00)80060-x
  • Primary Citation of Related Structures:  
    1B8C, 1B8L, 1B8R, 1B9A

  • PubMed Abstract: 

    The EF-hand family is a large set of Ca(2+)-binding proteins that contain characteristic helix-loop-helix binding motifs that are highly conserved in sequence. Members of this family include parvalbumin and many prominent regulatory proteins such as calmodulin and troponin C. EF-hand proteins are involved in a variety of physiological processes including cell-cycle regulation, second messenger production, muscle contraction, microtubule organization and vision.


  • Organizational Affiliation

    Department of Biochemistry and Cell Biology WM Keck Center for Computational Biology, Rice University, 6100 S. Main Street, Houston, TX 77005, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (PARVALBUMIN)108Cyprinus carpioMutation(s): 0 
UniProt
Find proteins for P02618 (Cyprinus carpio)
Explore P02618 
Go to UniProtKB:  P02618
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02618
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.177 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 28.85α = 90
b = 60.59β = 94.97
c = 54.48γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-02-09
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-04
    Changes: Refinement description
  • Version 1.4: 2018-03-07
    Changes: Data collection
  • Version 1.5: 2023-08-09
    Changes: Data collection, Database references, Derived calculations, Refinement description