The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of hydrolase haloacid dehalogenase-like family (np_662590.1) from Chlorobium tepidum TLS at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 2hcf Target Id 366871
    Molecular Characteristics
    Source Chlorobium tepidum tls
    Alias Ids TPS1484,NP_662590.1, 104741 Molecular Weight 25865.84 Da.
    Residues 233 Isoelectric Point 5.32
    Sequence msrtlvlfdidgtllkvesmnrrvladalievygtegstgshdfsgkmdgaiiyevlsnvgleraeiad kfdkaketyialfrerarreditllegvrelldalssrsdvllglltgnfeasgrhklklpgidhyfpf gafaddaldrnelphialerarrmtganyspsqiviigdtehdircareldarsiavatgnftmeelar hkpgtlfknfaetdevlasiltpkhs
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.80 Rfree 0.247
    Matthews' coefficent 2.01 Rfactor 0.189
    Waters 235 Solvent Content 38.41

    Ligand Information


    Google Scholar output for 2hcf
    1. Assessment of predictions submitted for the CASP7 function prediction category
    G Lopez, A Rojas, M Tress - : Structure, Function, and , 2007 - Wiley Online Library
    2. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
    3. Domain definition and target classification for CASP7
    ND Clarke, I Ezkurdia, J Kopp, RJ Read - Proteins: Structure, , 2007 - Wiley Online Library
    4. Modeling the resting state of oxalate oxidase and oxalate decarboxylase enzymes
    M Scarpellini, J Gtjens, OJ Martin, JW Kampf - Inorganic , 2008 - ACS Publications

    Protein Summary

    The gene NP_662590.1 from Chlorobium tepidum encodes a haloacid dehalogenase (HAD)-like hydrolase PF00702.  The enzyme belongs to the class of alpha and beta (a+b) proteins and adopts a HAD-like fold type SCOP56783. The HAD superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others, all of which use a nucleophilic aspartate in their phosphoryl transfer reaction. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable.  Several structures of the enzyme homologues from other organisms are available: 3KZXEhrlichia chaffeensis; 3KC2Saccharomyces cerevisiae.

    Ligand Summary





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