SCOPe 2.02: Domain d1krac2: 1kra C:130-422,C:476-567

Lineage for d1krac2 (1kra C:130-422,C:476-567)

1. Root: SCOPe 2.02

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 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] (19 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 Klebsiella aerogenes [TaxId:28451] [51562] (27 PDB entries)

8. Domain d1krac2: 1kra C:130-422,C:476-567 [29039]
   Other proteins in same PDB: d1kraa_, d1krab_, d1krac1
   mutant

Details for d1krac2

PDB Entry: 1kra, 2.3 Å

PDB Description: crystal structure of klebsiella aerogenes urease, its apoenzyme and two active site mutants

PDB Compounds: (C:) urease

SCOPe Domain Sequences for d1krac2:

Sequence; same for both SEQRES and ATOM records:

>d1krac2 c.1.9.2 (C:130-422,C:476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes [TaxId: 28451]}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglkihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf

Timeline for d1krac2:

• d1krac2 first appeared (with stable ids) in SCOP 1.55
  
• d1krac2 appears in SCOPe 2.01
  
• d1krac2 appears in SCOPe 2.03
  
• d1krac2 appears in the current release, SCOPe 2.08