PDBsum entry 1qhf

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Transferase PDB id
Protein chains
240 a.a. *
SO4 ×4
3PG ×2
Waters ×267
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a
Structure: Protein (phosphoglycerate mutase). Chain: a, b. Ec:
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932
Biol. unit: Tetramer (from PDB file)
1.70Å     R-factor:   0.177     R-free:   0.215
Authors: G.Crowhurst,J.Littlechild,H.C.Watson
Key ref:
G.S.Crowhurst et al. (1999). Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A. Acta Crystallogr D Biol Crystallogr, 55, 1822-1826. PubMed id: 10531478 DOI: 10.1107/S0907444999009944
13-May-99     Release date:   10-Jun-99    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P00950  (PMG1_YEAST) -  Phosphoglycerate mutase 1
247 a.a.
240 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2-phospho-D-glycerate = 3-phospho-D-glycerate
Bound ligand (Het Group name = 3PG)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   4 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     4 terms  


    Added reference    
DOI no: 10.1107/S0907444999009944 Acta Crystallogr D Biol Crystallogr 55:1822-1826 (1999)
PubMed id: 10531478  
Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.
G.S.Crowhurst, A.R.Dalby, M.N.Isupov, J.W.Campbell, J.A.Littlechild.
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.
  Selected figure(s)  
Figure 1.
Figure 1 Completeness of data and R[standard] of data plotted versus resolution. The figure was prepared using SFCHECK (Vaguine et al., 1999[Vaguine, A. A., Richelle, J. & Wodak, S. J. (1999). Acta Cryst. D55, 191-205.]).
Figure 4.
Figure 4 The 2F[o] - F[]c electron density (0.42 electrons per 3) surrounding the 3PG substrate after refinement. The sulfate anion is superimposed over the phosphate group. The 3PG and the sulfate have partial occupancies of 0.4 and 0.6, respectively. Figure drawn using O-PLOT (Jones et al., 1991[Jones, T. A., Zou, J. Y., Cowan, S. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.]).
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1822-1826) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
16615856 D.Hakobyan, and K.Nazaryan (2006).
Molecular dynamics simulation of interactions in glycolytic enzymes.
  Biochemistry (Mosc), 71, 370-375.  
16672613 H.A.Watkins, and E.N.Baker (2006).
Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.
  J Bacteriol, 188, 3589-3599.
PDB code: 2a6p
17052986 Y.Wang, L.Liu, Z.Wei, Z.Cheng, Y.Lin, and W.Gong (2006).
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.
  J Biol Chem, 281, 39642-39648.
PDB codes: 2a9j 2f90 2h4x 2h4z 2h52 2hhj
15258155 Y.Wang, Z.Wei, Q.Bian, Z.Cheng, M.Wan, L.Liu, and W.Gong (2004).
Crystal structure of human bisphosphoglycerate mutase.
  J Biol Chem, 279, 39132-39138.
PDB code: 1t8p
11114510 H.Erlandsen, E.E.Abola, and R.C.Stevens (2000).
Combining structural genomics and enzymology: completing the picture in metabolic pathways and enzyme active sites.
  Curr Opin Struct Biol, 10, 719-730.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.