3KBB

Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritima

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.74 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.191 
  • R-Value Observed: 0.194 

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This is version 1.2 of the entry. See complete history. 


Literature

Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima.

Strange, R.W., Antonyuk, S.V., Ellis, M.J., Bessho, Y., Kuramitsu, S., Shinkai, A., Yokoyama, S., Hasnain, S.S.

(2009) Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 1218-1221

  • DOI: https://doi.org/10.1107/S1744309109046302
  • Primary Citation of Related Structures:  
    3KBB

  • PubMed Abstract: 

    The structure of TM1254, a putative beta-phosphoglucomutase from T. maritima, was determined to 1.74 A resolution in a high-throughput structural genomics programme. Diffraction data were obtained from crystals belonging to space group P22(1)2(1), with unit-cell parameters a = 48.16, b = 66.70, c = 83.80 A, and were refined to an R factor of 19.2%. The asymmetric unit contained one protein molecule which is comprised of two domains. Structural homologues were found from protein databases that confirmed a strong resemblance between TM1254 and members of the haloacid dehalogenase (HAD) hydrolase family.

    • Organizational Affiliation: 

    Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, England. r.strange@liverpool.ac.uk


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Phosphorylated carbohydrates phosphatase TM_1254216Thermotoga maritima MSB8Mutation(s): 0 
Gene Names: bpgm, tm_1254
EC: 3.1.3
UniProt
Find proteins for Q9X0Y1 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9X0Y1 
Go to UniProtKB:  Q9X0Y1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X0Y1
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.74 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.191 
  • R-Value Observed: 0.194 
  • Space Group: P 2 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 48.16α = 90
b = 66.698β = 90
c = 83.8γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction
MAR345dtbdata collection
HKL-2000data reduction
HKL-2000data scaling
SHELXSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-11-17
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.2: 2017-11-01
    Changes: Refinement description