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* Residue conservation analysis
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Enzyme class:
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E.C.5.4.2.1
- Phosphoglycerate mutase.
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Reaction:
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2-phospho-D-glycerate = 3-phospho-D-glycerate
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2-phospho-D-glycerate
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=
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3-phospho-D-glycerate
Bound ligand (Het Group name = )
corresponds exactly
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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mitochondrion
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2 terms
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Biological process
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metabolic process
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3 terms
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Biochemical function
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catalytic activity
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5 terms
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DOI no:
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Acta Crystallogr D Biol Crystallogr
55:1822-1826
(1999)
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PubMed id:
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Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.
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G.S.Crowhurst,
A.R.Dalby,
M.N.Isupov,
J.W.Campbell,
J.A.Littlechild.
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ABSTRACT
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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.
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Selected figure(s)
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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.]).
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Figure 4.
Figure 4 The 2F[o] - F[]c electron density (0.42 electrons per
Å3) 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.]).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1999,
55,
1822-1826)
copyright 1999.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Hakobyan,
and
K.Nazaryan
(2006).
Molecular dynamics simulation of interactions in glycolytic enzymes.
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Biochemistry (Mosc), 71,
370-375.
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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.
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J Bacteriol, 188,
3589-3599.
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PDB code:
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Y.Wang,
L.Liu,
Z.Wei,
Z.Cheng,
Y.Lin,
and
W.Gong
(2006).
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.
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J Biol Chem, 281,
39642-39648.
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PDB codes:
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Y.Wang,
Z.Wei,
Q.Bian,
Z.Cheng,
M.Wan,
L.Liu,
and
W.Gong
(2004).
Crystal structure of human bisphosphoglycerate mutase.
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J Biol Chem, 279,
39132-39138.
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PDB code:
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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.
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Curr Opin Struct Biol, 10,
719-730.
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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.
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Links
