SCOP 1.65: Domain d4ubpc2: 4ubp C:132-434,C:484-570

Lineage for d4ubpc2 (4ubp C:132-434,C:484-570)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (26 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] (5 PDB entries)

8. Domain d4ubpc2: 4ubp C:132-434,C:484-570 [29053]
   Other proteins in same PDB: d4ubpa_, d4ubpb_, d4ubpc1
   complexed with ace, hae, ni

Details for d4ubpc2

PDB Entry: 4ubp, 1.55 Å

PDB Description: structure of bacillus pasteurii urease inhibited with acetohydroxamic acid at 1.55 a resolution

SCOP Domain Sequences for d4ubpc2:

Sequence; same for both SEQRES and ATOM records:

>d4ubpc2 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 d4ubpc2:

• d4ubpc2 first appeared (with stable ids) in SCOP 1.55
  
• d4ubpc2 appears in SCOP 1.63
  
• d4ubpc2 appears in SCOP 1.67
  
• d4ubpc2 appears in the current release, SCOPe 2.08