SCOPe 2.05: Domain d1o0qa1: 1o0q A:245-463

Lineage for d1o0qa1 (1o0q A:245-463)

1. Root: SCOPe 2.05

2. Class b: All beta proteins [48724] (176 folds)

3. Fold b.80: Single-stranded right-handed beta-helix [51125] (8 superfamilies)
   superhelix turns are made of parallel beta-strands and (short) turns

4. Superfamily b.80.7: beta-Roll [51120] (2 families)
   superhelix turns are made of two short strands each

5. Family b.80.7.1: Serralysin-like metalloprotease, C-terminal domain [51121] (1 protein)
   duplication: halfturs of beta-helix are sequence and structural repeats; binds calcium ions between the turns
   this is a repeat family; one repeat unit is 1go7 P:374-356 found in domain

6. Protein Metalloprotease [51122] (4 species)
   The catalytic N-terminal domain belong to the "zincin" superfamily

7. Species Pseudomonas sp., tac ii 18 [TaxId:306] [82190] (8 PDB entries)
   psychrophilic alkaline protease

8. Domain d1o0qa1: 1o0q A:245-463 [86536]
   Other proteins in same PDB: d1o0qa2
   complexed with ca, so4

Details for d1o0qa1

PDB Entry: 1o0q, 2.2 Å

PDB Description: Crystal structure of a cold adapted alkaline protease from Pseudomonas TAC II 18, co-crystallized with 1 mM EDTA

PDB Compounds: (A:) serralysin

SCOPe Domain Sequences for d1o0qa1:

Sequence; same for both SEQRES and ATOM records:

>d1o0qa1 b.80.7.1 (A:245-463) Metalloprotease {Pseudomonas sp., tac ii 18 [TaxId: 306]}
anletraddtvygfnstadrdfysatsstdklifsvwdgggndtldfsgfsqnqkinlta
gsfsdvggmtgnvsiaqgvtienaiggsgndlligndaanvlkggagndiiyggggadvl
wggtgsdtfvfgavsdstpkaadiikdfqsgfdkidltaitklgglnfvdaftghagdai
vsyhqasnagslqvdfsgqgvadflvttvgqvatydiva

Timeline for d1o0qa1:

• d1o0qa1 first appeared in SCOP 1.65
  
• d1o0qa1 appears in SCOPe 2.04
  
• d1o0qa1 appears in SCOPe 2.06
  
• d1o0qa1 appears in the current release, SCOPe 2.08