SCOP 1.69: Domain d1ubpc2: 1ubp C:132-434,C:484-570

Lineage for d1ubpc2 (1ubp C:132-434,C:484-570)

1. Root: SCOP 1.69

2. Class c: Alpha and beta proteins (a/b) [51349] (136 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (31 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] (13 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.1.9.2: alpha-subunit of urease, catalytic domain [51560] (1 protein)

6. Protein alpha-subunit of urease, catalytic domain [51561] (3 species)

7. Species Bacillus pasteurii [TaxId:1474] [51563] (6 PDB entries)

8. Domain d1ubpc2: 1ubp C:132-434,C:484-570 [29054]
   Other proteins in same PDB: d1ubpa_, d1ubpb_, d1ubpc1

Details for d1ubpc2

PDB Entry: 1ubp, 1.65 Å

PDB Description: crystal structure of urease from bacillus pasteurii inhibited with beta-mercaptoethanol at 1.65 angstroms resolution

SCOP Domain Sequences for d1ubpc2:

Sequence; same for both SEQRES and ATOM records:

>d1ubpc2 c.1.9.2 (C:132-434,C:484-570) alpha-subunit of urease, catalytic domain {Bacillus pasteurii}
ggidthvhfinpdqvdvalangittlfgggtgpaegskattvtpgpwniekmlksteglp
invgilgkghgssiapimeqidagaaglkihedwgatpasidrsltvadeadvqvaihsd
tlneagfledtlraingrvihsfhvegaggghapdimamaghpnvlpsstnptrpftvnt
idehldmlmvchhlkqnipedvafadsrirpetiaaedilhdlgiismmstdalamgrag
emvlrtwqtadkmkkqrgplaeekngsdnfrlkryvskytinpaiaqgiahevgsieegk
fadXgdlihdtnitfmskssiqqgvpaklglkrrigtvkncrnigkkdmkwndvttdidi
npetyevkvdgevltcepvkelpmaqryflf

Timeline for d1ubpc2:

• d1ubpc2 first appeared (with stable ids) in SCOP 1.55
  
• d1ubpc2 appears in SCOP 1.67
  
• d1ubpc2 appears in SCOP 1.71
  
• d1ubpc2 appears in the current release, SCOPe 2.08