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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 catalytic domain of dual specificity ph 26, ms0830 from homo sapiens
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Structure:
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Dual specificity phosphatase 26. Chain: a. Fragment: catalytic domain, residues 61-211. Synonym: ms0830, putative, low-molecular-mass dual- specifi phosphatase 4, dual-specificity phosphatase skrp3, mitogen- protein kinase phosphatase 8, nata1 protein, cdna flj31142 imr322001317, weakly similar to homo sapiens protein phosph engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Other_details: cell-free protein synthesis
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Resolution:
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1.67Å
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R-factor:
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0.172
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R-free:
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0.212
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Authors:
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Y.Xie,S.Kishishita,K.Murayama,C.Hori-Takemoto,L.Chen,Z.J.Liu B.C.Wang,M.Shirozu,S.Yokoyama,Riken Structural Genomics/pro Initiative (Rsgi)
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Key ref:
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Y.Xie
et al.
Crystal structure of catalytic domain of dual specificity phosphatase 26, Ms0830 from homo sapiens.
To be published,
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Date:
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13-Oct-06
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Release date:
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16-Oct-07
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PROCHECK
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Headers
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References
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Q9BV47
(DUS26_HUMAN) -
Dual specificity protein phosphatase 26
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Seq: Struc:
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211 a.a.
150 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class 2:
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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 3:
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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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3 terms
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