3TMJ

Joint X-ray/neutron structure of human carbonic anhydrase II at pH 7.8


Experimental Data Snapshot

  • Method: NEUTRON DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.294 
  • R-Value Work: 0.280 

    wwPDB Validation   3D Report Full Report


    This is version 1.4 of the entry. See complete history


    Literature

    Neutron Structure of Human Carbonic Anhydrase II: A Hydrogen-Bonded Water Network "Switch" Is Observed between pH 7.8 and 10.0.

    Fisher, Z.Kovalevsky, A.Y.Mustyakimov, M.Silverman, D.N.McKenna, R.Langan, P.

    (2011) Biochemistry 50: 9421-9423

    • DOI: https://doi.org/10.1021/bi201487b
    • Primary Citation of Related Structures:  
      3TMJ

    • PubMed Abstract: 

      The neutron structure of wild-type human carbonic anhydrase II at pH 7.8 has been determined to 2.0 Å resolution. Detailed analysis and comparison to the previously determined structure at pH 10.0 show important differences in the protonation of key catalytic residues in the active site as well as a rearrangement of the H-bonded water network. For the first time, a completed H-bonded network stretching from the Zn-bound solvent to the proton shuttling residue, His64, has been directly observed.


    • Organizational Affiliation

      Bioscience Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87544, United States. zfisher@lanl.gov


    Macromolecules
    Find similar proteins by:  (by identity cutoff)  |  3D Structure
    Entity ID: 1
    MoleculeChains Sequence LengthOrganismDetailsImage
    Carbonic anhydrase 2258Homo sapiensMutation(s): 0 
    Gene Names: CA2
    EC: 4.2.1.1
    UniProt & NIH Common Fund Data Resources
    Find proteins for P00918 (Homo sapiens)
    Explore P00918 
    Go to UniProtKB:  P00918
    PHAROS:  P00918
    GTEx:  ENSG00000104267 
    Entity Groups  
    Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
    UniProt GroupP00918
    Sequence Annotations
    Expand
    • Reference Sequence
    Small Molecules
    Ligands 1 Unique
    IDChains Name / Formula / InChI Key2D Diagram3D Interactions
    ZN
    Query on ZN

    Download Ideal Coordinates CCD File 
    B [auth A]ZINC ION
    Zn
    PTFCDOFLOPIGGS-UHFFFAOYSA-N
    Experimental Data & Validation

    Experimental Data

    • Method: NEUTRON DIFFRACTION
    • Resolution: 2.00 Å
    • R-Value Free: 0.294 
    • R-Value Work: 0.280 
    • Space Group: P 1 21 1
    Unit Cell:
    Length ( Å )Angle ( ˚ )
    a = 42.83α = 90
    b = 41.7β = 104.58
    c = 72.92γ = 90
    Software Package:
    Software NamePurpose
    PCSdata collection
    nCNSrefinement
    d*TREKdata reduction
    SCALAdata scaling
    d*TREKdata scaling
    nCNSphasing

    Structure Validation

    View Full Validation Report



    Entry History 

    Deposition Data

    • Released Date: 2011-11-09 
    • Deposition Author(s): Fisher, Z.

    Revision History  (Full details and data files)

    • Version 1.0: 2011-11-09
      Type: Initial release
    • Version 1.1: 2017-11-08
      Changes: Refinement description
    • Version 1.2: 2018-04-25
      Changes: Data collection
    • Version 1.3: 2018-06-13
      Changes: Data collection
    • Version 1.4: 2023-09-13
      Changes: Data collection, Database references, Derived calculations, Refinement description