SCOPe 2.05: Domain d2nylc1: 2nyl C:2-294

Lineage for d2nylc1 (2nyl C:2-294)

1. Root: SCOPe 2.05

2. Class d: Alpha and beta proteins (a+b) [53931] (381 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 d2nylc1: 2nyl C:2-294 [138817]
   Other proteins in same PDB: d2nyla1, d2nylb1, d2nyld1, d2nyle1
   complexed with mn

Details for d2nylc1

PDB Entry: 2nyl, 3.8 Å

PDB Description: crystal structure of protein phosphatase 2a (pp2a) holoenzyme with the catalytic subunit carboxyl terminus truncated

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

SCOPe Domain Sequences for d2nylc1:

Sequence; same for both SEQRES and ATOM records:

>d2nylc1 d.159.1.3 (C:2-294) Protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha {Human (Homo sapiens) [TaxId: 9606]}
dekvftkeldqwieqlneckqlsesqvkslcekakeiltkesnvqevrcpvtvcgdvhgq
fhdlmelfriggkspdtnylfmgdyvdrgyysvetvtllvalkvryreritilrgnhesr
qitqvygfydeclrkygnanvwkyftdlfdylpltalvdgqifclhgglspsidtldhir
aldrlqevphegpmcdllwsdpddrggwgisprgagytfgqdisetfnhangltlvsrah
qlvmegynwchdrnvvtifsapnycyrcgnqaaimelddtlkysflqfdpapr

Timeline for d2nylc1:

• d2nylc1 first appeared in SCOP 1.73
  
• d2nylc1 appears in SCOPe 2.04
  
• d2nylc1 appears in SCOPe 2.06
  
• d2nylc1 appears in the current release, SCOPe 2.08