Class d: Alpha and beta proteins (a+b) [53931] (396 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 Presequence protease 1, PREP1 [143498] (1 species) duplication: comprises four domains of this fold; similar to the MPP alpha-beta heterodimer |
Species Thale cress (Arabidopsis thaliana) [TaxId:3702] [143499] (1 PDB entry) Uniprot Q9LJL3 100-356! Uniprot Q9LJL3 357-624! Uniprot Q9LJL3 625-882! Uniprot Q9LJL3 883-1078 |
Domain d2fgeb3: 2fge B:272-539 [133436] automated match to d2fgea3 complexed with cl, mg, zn |
PDB Entry: 2fge (more details), 2.1 Å
SCOPe Domain Sequences for d2fgeb3:
Sequence; same for both SEQRES and ATOM records: (download)
>d2fgeb3 d.185.1.1 (B:272-539) Presequence protease 1, PREP1 {Thale cress (Arabidopsis thaliana) [TaxId: 3702]} fqklfsepvrlvekypagrdgdlkkkhmlcvnwllsekpldlqtqlalgfldhlmlgtpa splrkillesglgealvssglsdellqpqfgiglkgvseenvqkveelimdtlkklaeeg fdndaveasmntiefslrenntgsfprglslmlqsiskwiydmdpfeplkyteplkalkt riaeegskavfsplieklilnnshrvtiemqpdpekatqeeveeknilekvkaamteedl aelarateelklkqetpdppealrcvps
Timeline for d2fgeb3:
View in 3D Domains from other chains: (mouse over for more information) d2fgea1, d2fgea2, d2fgea3, d2fgea4 |