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Contents |
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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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Protein tyrosine phosphatase, receptor type, e isoform
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Structure:
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Receptor-type tyrosine-protein phosphatase epsilo chain: a, b, c, d, e, f. Fragment: residues 107-697. Synonym: protein-tyrosine phosphatase epsilon, r-ptp -epsil protein tyrosine phosphatase, receptor type, e isoform. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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3.20Å
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R-factor:
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0.223
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R-free:
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0.256
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Authors:
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J.M.Elkins,E.Ugochukwu,I.Alfano,A.J.Barr,G.Bunkoczi,O.N.F.Ki P.Filippakopoulos,P.Savitsky,E.Salah,A.Pike,C.Johansson,S.D N.A.Burgess-Brown,O.Gileadi,F.Vondelft,C.H.Arrowsmith,C.Bou A.M.Edwards,S.Knapp
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Key ref:
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A.Barr
Structure of human ptpre.
To be published,
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Date:
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31-Mar-08
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Release date:
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08-Apr-08
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PROCHECK
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Headers
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References
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P23469
(PTPRE_HUMAN) -
Receptor-type tyrosine-protein phosphatase epsilon
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Seq:
Struc:
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700 a.a.
537 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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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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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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Links
