SCOPe 2.06: Domain d2qs8a2: 2qs8 A:64-373

Lineage for d2qs8a2 (2qs8 A:64-373)

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.9: Metallo-dependent hydrolases [51556] (19 families)
   the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
   has transition metal ions bound inside the barrel

5. Family c.1.9.18: Zn-dependent arginine carboxypeptidase-like [159408] (3 proteins)
   automatically mapped to Pfam PF01979

6. Protein Xaa-Pro dipeptidase [159409] (1 species)

7. Species Alteromonas macleodii [TaxId:28108] [159410] (1 PDB entry)

8. Domain d2qs8a2: 2qs8 A:64-373 [151312]
   Other proteins in same PDB: d2qs8a1, d2qs8a3, d2qs8b1
   complexed with met, mg

Details for d2qs8a2

PDB Entry: 2qs8, 2.33 Å

PDB Description: crystal structure of a xaa-pro dipeptidase with bound methionine in the active site

PDB Compounds: (A:) Xaa-Pro Dipeptidase

SCOPe Domain Sequences for d2qs8a2:

Sequence; same for both SEQRES and ATOM records:

>d2qs8a2 c.1.9.18 (A:64-373) Xaa-Pro dipeptidase {Alteromonas macleodii [TaxId: 28108]}
glmdmhvhfgqeyqskaqapikveremqailatqhayvtfksgfttvrqvgdsglvaisl
rdainsgklagprifaagktiattgghadptngkavddydypvpeqgvvngpyevyaavr
qrykdgadgikitvtggvlsvaksgqnpqftqeevdavvsaakdygmwvavhahgaegmk
raikagvdsiehgtfmdleamdlmiengtyyvptisagefvaekskidnffpeivrpkaa
svgpqisdtfrkayekgvkiafgtdagvqkhgtnwkefvymvengmpamkaiqsatmeta
kllriedklg

Timeline for d2qs8a2:

• d2qs8a2 first appeared in SCOP 1.75
  
• d2qs8a2 appears in SCOPe 2.05
  
• d2qs8a2 appears in SCOPe 2.07
  
• d2qs8a2 appears in the current release, SCOPe 2.08