Lineage for d1fpra_ (1fpr A:)

  1. Root: SCOP 1.71
  2. 570216Class c: Alpha and beta proteins (a/b) [51349] (134 folds)
  3. 584246Fold c.45: (Phosphotyrosine protein) phosphatases II [52798] (1 superfamily)
    core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1423
  4. 584247Superfamily c.45.1: (Phosphotyrosine protein) phosphatases II [52799] (4 families) (S)
    share with the family I the common active site structure with a circularly permuted topology
  5. 584295Family c.45.1.2: Higher-molecular-weight phosphotyrosine protein phosphatases [52805] (6 proteins)
    has an extension to the beta-sheet of 3 antiparallel strands before strand 4
  6. 584321Protein Tyrosine phosphatase [52806] (7 species)
  7. 584397Species Human (Homo sapiens), shp-1 [TaxId:9606] [52811] (2 PDB entries)
  8. 584398Domain d1fpra_: 1fpr A: [59949]
    complex with an in vitro peptide substrate py469 derived from shps-1, chain B
    mutant

Details for d1fpra_

PDB Entry: 1fpr (more details), 2.5 Å

PDB Description: crystal structure of the complex formed between the catalytic domain of shp-1 and an in vitro peptide substrate py469 derived from shps-1.

SCOP Domain Sequences for d1fpra_:

Sequence; same for both SEQRES and ATOM records: (download)

>d1fpra_ c.45.1.2 (A:) Tyrosine phosphatase {Human (Homo sapiens), shp-1}
gfweefeslqkqevknlhqrlegqrpenkgknryknilpfdhsrvilqgrdsnipgsdyi
nanyiknqllgpdenaktyiasqgcleatvndfwqmawqensrvivmttrevekgrnkcv
pywpevgmqraygpysvtncgehdtteyklrtlqvspldngdlireiwhyqylswpdhgv
psepggvlsfldqinqrqeslphagpiivhssagigrtgtiividmlmenistkgldcdi
diqktiqmvraqrsgmvqteaqykfiyvaiaqfiettkkklevl

SCOP Domain Coordinates for d1fpra_:

Click to download the PDB-style file with coordinates for d1fpra_.
(The format of our PDB-style files is described here.)

Timeline for d1fpra_: