SCOPe 2.07: Domain d2ie3c1: 2ie3 C:6-293

Lineage for d2ie3c1 (2ie3 C:6-293)

1. Root: SCOPe 2.07

2. Class d: Alpha and beta proteins (a+b) [53931] (388 folds)

3. Fold d.159: Metallo-dependent phosphatases [56299] (1 superfamily)
   4 layers: alpha/beta/beta/alpha; mixed beta sheets; contains duplication

4. Superfamily d.159.1: Metallo-dependent phosphatases [56300] (13 families)
   different families of this superfamily are groupped in a single Pfam family, Pfam PF00149

5. Family d.159.1.3: Protein serine/threonine phosphatase [56310] (6 proteins)

6. Protein Protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha [143933] (1 species)

7. Species Human (Homo sapiens) [TaxId:9606] [143934] (12 PDB entries)
   Uniprot P67775 2-294

8. Domain d2ie3c1: 2ie3 C:6-293 [145523]
   Other proteins in same PDB: d2ie3a_
   complexed with mn

Details for d2ie3c1

PDB Entry: 2ie3, 2.8 Å

PDB Description: Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins

PDB Compounds: (C:) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

SCOPe Domain Sequences for d2ie3c1:

Sequence; same for both SEQRES and ATOM records:

>d2ie3c1 d.159.1.3 (C:6-293) Protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha {Human (Homo sapiens) [TaxId: 9606]}
ftkeldqwieqlneckqlsesqvkslcekakeiltkesnvqevrcpvtvcgdvhgqfhdl
melfriggkspdtnylfmgdyvdrgyysvetvtllvalkvryreritilrgnhesrqitq
vygfydeclrkygnanvwkyftdlfdylpltalvdgqifclhgglspsidtldhiraldr
lqevphegpmcdllwsdpddrggwgisprgagytfgqdisetfnhangltlvsrahqlvm
egynwchdrnvvtifsapnycyrcgnqaaimelddtlkysflqfdpap

Timeline for d2ie3c1:

• d2ie3c1 first appeared in SCOP 1.75
  
• d2ie3c1 appears in SCOPe 2.06
  
• d2ie3c1 appears in the current release, SCOPe 2.08