SCOPe 2.08: Domain d1bpma1: 1bpm A:160-484

Lineage for d1bpma1 (1bpm A:160-484)

1. Root: SCOPe 2.08

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

3. Fold c.56: Phosphorylase/hydrolase-like [53162] (8 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] (10 families)
   core: mixed beta-sheet of 8 strands, order 12435867; strands 2, 6 & 7 are antiparallel to the rest

5. Family c.56.5.3: Leucine aminopeptidase, C-terminal domain [53201] (2 proteins)
   automatically mapped to Pfam PF00883

6. Protein Leucine aminopeptidase, C-terminal domain [53202] (2 species)

7. Species Cow (Bos taurus) [TaxId:9913] [53203] (7 PDB entries)

8. Domain d1bpma1: 1bpm A:160-484 [33835]
   Other proteins in same PDB: d1bpma2
   complexed with mg, zn

Details for d1bpma1

PDB Entry: 1bpm, 2.9 Å

PDB Description: differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography

PDB Compounds: (A:) leucine aminopeptidase

SCOPe Domain Sequences for d1bpma1:

Sequence; same for both SEQRES and ATOM records:

>d1bpma1 c.56.5.3 (A:160-484) Leucine aminopeptidase, C-terminal domain {Cow (Bos taurus) [TaxId: 9913]}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq

Timeline for d1bpma1:

• d1bpma1 first appeared (with stable ids) in SCOP 1.55, called d1bpm_2
  
• d1bpma1 appears in SCOPe 2.07