1RII

Crystal structure of phosphoglycerate mutase from M. Tuberculosis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.270 
  • R-Value Observed: 0.219 

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This is version 1.4 of the entry. See complete history


Literature

The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.

Muller, P.Sawaya, M.R.Pashkov, I.Chan, S.Nguyen, C.Wu, Y.Perry, L.J.Eisenberg, D.

(2005) Acta Crystallogr D Biol Crystallogr 61: 309-315

  • DOI: https://doi.org/10.1107/S0907444904033190
  • Primary Citation of Related Structures:  
    1RII

  • PubMed Abstract: 

    The single-crystal X-ray structure of phosphoglycerate mutase from Mycobacterium tuberculosis has been determined at a resolution of 1.70 angstroms. The C-terminal tail of each of the subunits is flexible and disordered; however, for one of the four chains (chain A) all but five residues of the chain could be modeled. Noteworthy features of the structure include the active site and a proline-rich segment in each monomer forming a short left-handed polyprolyl helix. These segments lie on the enzyme surface and could conceivably participate in protein-protein interactions.


  • Organizational Affiliation

    UCLA-DOE Institute for Genomics and Proteomics, Howard Hughes Medical Institute, Box 951570, Los Angeles, CA 90095-1570, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
A, B, C, D
265Mycobacterium tuberculosisMutation(s): 0 
Gene Names: GPMAGPMPGMGPM1RV0489MT0508MTCY20G9.15MB0499
EC: 5.4.2.1
UniProt
Find proteins for P9WIC9 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WIC9 
Go to UniProtKB:  P9WIC9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WIC9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.270 
  • R-Value Observed: 0.219 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 58.914α = 90
b = 136.79β = 97.78
c = 65.929γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SADABSdata reduction
GLRFphasing
SHELXL-97refinement
SADABSdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-10-05
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.3: 2017-10-11
    Changes: Refinement description
  • Version 1.4: 2023-08-23
    Changes: Data collection, Database references, Derived calculations, Refinement description