1QHF

YEAST PHOSPHOGLYCERATE MUTASE-3PG COMPLEX STRUCTURE TO 1.7 A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.177 

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This is version 1.3 of the entry. See complete history


Literature

Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.

Crowhurst, G.S.Dalby, A.R.Isupov, M.N.Campbell, J.W.Littlechild, J.A.

(1999) Acta Crystallogr D Biol Crystallogr 55: 1822-1826

  • DOI: https://doi.org/10.1107/s0907444999009944
  • Primary Citation of Related Structures:  
    1QHF

  • PubMed Abstract: 

    The crystal structure of the tetrameric glycolytic enzyme phosphoglycerate mutase from the yeast Saccharomyces cerevisiae has been determined to 1.7 A resolution in complex with the sugar substrate. The difference map indicates that 3-phosphoglycerate is bound at the base of a 12 A cleft, positioning C2 of the substrate within 3.5 A of the primary catalytic residue, histidine 8.


  • Organizational Affiliation

    Schools of Chemistry, University of Exeter, Stocker Road, Exeter, Devon EX4 4QD, England.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (PHOSPHOGLYCERATE MUTASE)
A, B
240Saccharomyces cerevisiaeMutation(s): 0 
EC: 5.4.2.1
UniProt
Find proteins for P00950 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P00950 
Go to UniProtKB:  P00950
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00950
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.177 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 96.4α = 90
b = 85.9β = 120.6
c = 81.9γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-06-10
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-16
    Changes: Data collection, Database references, Derived calculations, Refinement description