SCOP 1.73: Domain d2prqa1: 2prq A:1-291

Lineage for d2prqa1 (2prq A:1-291)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 folds)

3. Fold c.56: Phosphorylase/hydrolase-like [53162] (7 superfamilies)
   core: 3 layers, a/b/a ; mixed sheet of 5 strands: order 21354; strand 4 is antiparallel to the rest; contains crossover loops

4. Superfamily c.56.5: Zn-dependent exopeptidases [53187] (8 families)
   core: mixed beta-sheet of 8 strands, order 12435867; strands 2, 6 & 7 are antiparallel to the rest

5. Family c.56.5.4: Bacterial dinuclear zinc exopeptidases [53204] (17 proteins)

6. Protein Aminopeptidase [53205] (2 species)

7. Species Aeromonas proteolytica [TaxId:671] [53206] (11 PDB entries)
   synonym: Vibrio proteolyticus

8. Domain d2prqa1: 2prq A:1-291 [139750]
   automatically matched to d1amp__
   complexed with co, trs

Details for d2prqa1

PDB Entry: 2prq, 2.15 Å

PDB Description: x-ray crystallographic characterization of the co(ii)-substituted tris-bound form of the aminopeptidase from aeromonas proteolytica

PDB Compounds: (A:) Bacterial leucyl aminopeptidase

SCOP Domain Sequences for d2prqa1:

Sequence; same for both SEQRES and ATOM records:

>d2prqa1 c.56.5.4 (A:1-291) Aminopeptidase {Aeromonas proteolytica [TaxId: 671]}
mppitqqatvtawlpqvdasqitgtisslesftnrfytttsgaqasdwiasewqalsasl
pnasvkqvshsgynqksvvmtitgseapdewivigghldstigshtneqsvapgadddas
giaavtevirvlsennfqpkrsiafmayaaeevglrgsqdlanqyksegknvvsalqldm
tnykgsaqdvvfitdytdsnftqyltqlmdeylpsltygfdtcgyacsdhaswhnagypa
ampfeskfndynprihttqdtlansdptgshakkftqlglayaiemgsatg

Timeline for d2prqa1:

• d2prqa1 is new in SCOP 1.73
  
• d2prqa1 appears in SCOP 1.75
  
• d2prqa1 appears in the current release, SCOPe 2.08, called d2prqa_