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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of dusp15
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Structure:
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Dual specificity phosphatase-like 15 isoform a. Chain: a, b. Fragment: catalytic domain. Synonym: dusp15. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.40Å
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R-factor:
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0.217
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R-free:
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0.269
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Authors:
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S.J.Kim,S.E.Ryu,D.G.Jeong,T.S.Yoon,J.H.Kim,Y.H.Cho, S.K.Jeong,J.W.Lee,J.H.Son
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Key ref:
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T.S.Yoon
et al.
(2005).
Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase.
Proteins,
61,
694-697.
PubMed id:
DOI:
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Date:
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28-Feb-05
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Release date:
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01-Nov-05
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PROCHECK
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Headers
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References
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Q9H1R2
(DUS15_HUMAN) -
Dual specificity protein phosphatase 15
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Seq: Struc:
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295 a.a.
159 a.a.*
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Key: |
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PfamA domain |
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PfamB domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 12 residue positions (black
crosses)
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Enzyme class 1:
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E.C.3.1.3.16
- Phosphoprotein phosphatase.
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Reaction:
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A phosphoprotein + H2O = a protein + phosphate
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phosphoprotein
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+
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H(2)O
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=
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protein
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+
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phosphate
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Enzyme class 2:
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E.C.3.1.3.48
- Protein-tyrosine-phosphatase.
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Reaction:
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Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
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Protein tyrosine phosphate
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+
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H(2)O
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=
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protein tyrosine
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+
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phosphate
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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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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Biological process
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dephosphorylation
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2 terms
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Biochemical function
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phosphatase activity
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2 terms
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DOI no:
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Proteins
61:694-697
(2005)
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PubMed id:
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Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase.
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T.S.Yoon,
D.G.Jeong,
J.H.Kim,
Y.H.Cho,
J.H.Son,
J.W.Lee,
S.E.Ryu,
S.J.Kim.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. (a) The VHYc structure represented as a ribbon
diagram. Secondary structural elements are labeled on the
drawing. The bound sulfate ion is represented as a
ball-and-stick model. (b) C trace
of the VHYc structure (thick line) is superimposed with that of
the VHR structure (thin line). The regions of VHYc that cannot
be aligned are colored green, whereas the regions of VHYc that
are missing are colored red. The point of view is the same as
that in (a). (c) Electrostatic potential surfaces of VHYc and
VHR are presented. Positive and negative potentials are colored
blue and red, respectively. The point of view is the same as
that in (a).
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The above figure is
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
61,
694-697)
copyright 2005.
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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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J.P.Li,
Y.N.Fu,
Y.R.Chen,
and
T.H.Tan
(2010).
JNK pathway-associated phosphatase dephosphorylates focal adhesion kinase and suppresses cell migration.
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J Biol Chem, 285,
5472-5478.
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H.M.Chu,
and
A.H.Wang
(2007).
Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes.
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Proteins, 66,
996.
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PDB codes:
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J.Phan,
J.E.Tropea,
and
D.S.Waugh
(2007).
Structure-assisted discovery of Variola major H1 phosphatase inhibitors.
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Acta Crystallogr D Biol Crystallogr, 63,
698-704.
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PDB code:
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S.K.Jung,
D.G.Jeong,
T.S.Yoon,
J.H.Kim,
S.E.Ryu,
and
S.J.Kim
(2007).
Crystal structure of human slingshot phosphatase 2.
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Proteins, 68,
408-412.
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PDB code:
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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
codes are
shown on the right.
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