Class d: Alpha and beta proteins (a+b) [53931] (380 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 d1hr7a2: 1hr7 A:234-470 [61181] Other proteins in same PDB: d1hr7b1, d1hr7b2, d1hr7d1, d1hr7d2, d1hr7f1, d1hr7f2, d1hr7h1, d1hr7h2 complexed with zn; mutant |
PDB Entry: 1hr7 (more details), 2.55 Å
SCOPe Domain Sequences for d1hr7a2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1hr7a2 d.185.1.1 (A:234-470) Mitochondrial processing peptidase (MPP) alpha chain {Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]} vaqytggescippapvfgnlpelfhiqigfeglpidhpdiyalatlqtllggggsfsagg pgkgmysrlythvlnqyyfvencvafnhsysdsgifgislscipqaapqaveviaqqmyn tfankdlrltedevsraknqlkssllmnlesklveledmgrqvlmhgrkipvnemiskie dlkpddisrvaemiftgnvnnagngkgratvvmqgdrgsfgdvenvlkayglgnsss
Timeline for d1hr7a2: