Structural Classification of Proteins
Family: Higher-molecular-weight phosphotyrosine protein phosphatases
has an extension to the beta-sheet of 3 antiparallel strands before strand 4
Lineage:
Root:
scop
Class:
Alpha and beta proteins (a/b)
[51349]
Mainly parallel beta sheets (beta-alpha-beta units)
Fold:
(Phosphotyrosine protein) phosphatases II
[52798]
core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1423
Superfamily:
(Phosphotyrosine protein) phosphatases II
[52799]
share with the family I the common active site structure with a circularly permuted topology
uperfamily
Family:
Higher-molecular-weight phosphotyrosine protein phosphatases
[52805]
has an extension to the beta-sheet of 3 antiparallel strands before strand 4
Protein Domains:
Tyrosine phosphatase [52806]
Human (Homo sapiens), 1B
[TaxId: 9606]
[52807] (92)
SQ
P18031
2-300 ! SQ
P18031
1-298 ! SQ
P18031
2-299
Human (Homo sapiens), mu
[TaxId: 9606]
[52808] (1)
receptor protein tyrosine phosphatase mu, domain 1
Mouse (Mus musculus)
[TaxId: 10090]
[52809] (1)
receptor protein tyrosine phosphatase alpha, domain 1
Human (Homo sapiens), shp-2
[TaxId: 9606]
[52810] (1)
Human (Homo sapiens), shp-1
[TaxId: 9606]
[52811] (2)
Mouse (Mus musculus), ptp-sl/br7
[TaxId: 10090]
[64051] (1)
Human (Homo sapiens), T-cell
[TaxId: 9606]
[75233] (1)
non-receptor type 2
Protein-tyrosine phosphatase YopH, catalytic domain [100952]
Yersinia enterocolitica
[TaxId: 630]
[52812] (13)
SptP tyrosine phosphatase, catalytic domain [52813]
Salmonella typhimurium
[TaxId: 90371]
[52814] (2)
RPTP Lar [52815]
duplication: tandem repeat of the phosphatase domain
Human (Homo sapiens)
[TaxId: 9606]
[52816] (1)
Protein-tyrosine phosphatase alpha [102420]
Mouse (Mus musculus)
[TaxId: 10090]
[102421] (1)
Tyrosine-protein phosphatase, non-receptor type 13 (PTPL1) [117581]
Human (Homo sapiens)
[TaxId: 9606]
[117582] (1)
SQ
Q12923
2170-2477 # structure of a PDZ domain (1361-1456) is also known (
scop_sp 50169
)
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Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright
© 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk