SCOP 1.63: Domain d1gkrd2: 1gkr D:55-379

Lineage for d1gkrd2 (1gkr D:55-379)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 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] (12 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.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (2 proteins)

6. Protein L-hydantoinase [75077] (1 species)

7. Species Arthrobacter aurescens [TaxId:43663] [75078] (1 PDB entry)

8. Domain d1gkrd2: 1gkr D:55-379 [70258]
   Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
   complexed with kcx, zn

Details for d1gkrd2

PDB Entry: 1gkr, 2.6 Å

PDB Description: l-hydantoinase (dihydropyrimidinase) from arthrobacter aurescens

SCOP Domain Sequences for d1gkrd2:

Sequence; same for both SEQRES and ATOM records:

>d1gkrd2 c.1.9.6 (D:55-379) L-hydantoinase {Arthrobacter aurescens}
gvvdehvhiidmdlknrygrfeldsesaavggittiiempitfpptttldaflekkkqag
qrlkvdfalygggvpgnlpeirkmhdagavgfksmmaasvpgmfdavsdgelfeifqeia
acgsvivvhaenetiiqalqkqikaaggkdmaayeasqpvfqeneaiqralllqkeagcr
livlhvsnpdgvelihqaqsegqdvhcesgpqylnittddaerigpymkvappvrsaemn
irlweqlenglidtlgsdhgghpvedkepgwkdvwkagngalgletslpmmltngvnkgr
lslerlvevmcekpaklfgiypqkg

Timeline for d1gkrd2:

• d1gkrd2 first appeared in SCOP 1.61
  
• d1gkrd2 appears in SCOP 1.65
  
• d1gkrd2 appears in the current release, SCOPe 2.08