1V9E

Crystal Structure Analysis of Bovine Carbonic Anhydrase II


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.270 

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This is version 1.3 of the entry. See complete history


Literature

Structure of bovine carbonic anhydrase II at 1.95 A resolution.

Saito, R.Sato, T.Ikai, A.Tanaka, N.

(2004) Acta Crystallogr D Biol Crystallogr 60: 792-795

  • DOI: https://doi.org/10.1107/S0907444904003166
  • Primary Citation of Related Structures:  
    1V9E

  • PubMed Abstract: 

    Carbonic anhydrase (CA) is a zinc-containing enzyme that catalyzes the reversible hydration of CO2 to HCO3-. In eukaryotes, the enzyme plays a role in various physiological functions, including interconversion between CO2 and HCO3- in intermediary metabolism, facilitated diffusion of CO2, pH homeostasis and ion transport. The structure of bovine carbonic anhydrase II (BCA II) has been determined by molecular replacement and refined to 1.95 A resolution by simulated-annealing and individual B-factor refinement. The final R factor for the BCA II structure was 19.4%. BCA II has a C-terminal knot structure similar to that observed in human CA II. It contains one zinc ion in the active site coordinated to three histidines and one putative water molecule in a tetrahedral geometry. The structure of BCA II reveals a probable alternative proton-wire pathway that differs from that of HCA II.


  • Organizational Affiliation

    Department of Life Science, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Japan.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbonic anhydrase II
A, B
259Bos taurusMutation(s): 0 
EC: 4.2.1.1
UniProt
Find proteins for P00921 (Bos taurus)
Explore P00921 
Go to UniProtKB:  P00921
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00921
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.270 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 66.7α = 90
b = 66.7β = 90
c = 240γ = 120
Software Package:
Software NamePurpose
CNSrefinement
MOSFLMdata reduction
CCP4data scaling
EPMRphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-02-10
    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: 2023-12-27
    Changes: Data collection, Database references, Derived calculations