![]() | Class d: Alpha and beta proteins (a+b) [53931] (388 folds) |
![]() | Fold d.185: LuxS/MPP-like metallohydrolase [63410] (1 superfamily) core: beta-alpha-beta(2)-alpha(2); 2 layers: alpha/beta |
![]() | Superfamily d.185.1: LuxS/MPP-like metallohydrolase [63411] (3 families) ![]() Share the same "active site motif" HxxEH located in the first core helix, but differ in one of the zinc-binding residues |
![]() | Family d.185.1.1: MPP-like [63412] (7 proteins) Common fold elaborated with many additional structures; duplication: each family member consists of two similar domains of beta(2)-alpha(2)-beta(2)-alpha(5)-beta structure, but only the N-terminal domain of MPP beta chain binds the catalytic metal |
![]() | Protein Mitochondrial processing peptidase (MPP) alpha chain [64302] (1 species) |
![]() | Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [64303] (4 PDB entries) |
![]() | Domain d1hr9e1: 1hr9 E:14-233 [61220] Other proteins in same PDB: d1hr9b1, d1hr9b2, d1hr9d1, d1hr9d2, d1hr9f1, d1hr9f2, d1hr9f3, d1hr9h1, d1hr9h2 complexed with epe, zn; mutant |
PDB Entry: 1hr9 (more details), 3.01 Å
SCOPe Domain Sequences for d1hr9e1:
Sequence; same for both SEQRES and ATOM records: (download)
>d1hr9e1 d.185.1.1 (E:14-233) Mitochondrial processing peptidase (MPP) alpha chain {Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]} artdnfklsslanglkvatsntpghfsalglyidagsrfegrnlkgcthildrlafkste hvegramaetlellggnyqctssrenlmyqasvfnqdvgkmlqlmsetvrfpkiteqelq eqklsaeyeidevwmkpelvlpellhtaaysgetlgsplicprglipsiskyylldyrnk fytpentvaafvgvphekaleltgkylgdwqsthppitkk
Timeline for d1hr9e1: