Lineage for Protein: Protease III
- Root: SCOPe 2.07
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/betaSuperfamily 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 Protease III [143500] (1 species)
duplication: comprises four domains of this fold
Species:
Escherichia coli [TaxId:562] [143501] (1 PDB entry)
Uniprot P05458 24-263! Uniprot P05458 264-503! Uniprot P05458 504-732! Uniprot P05458 733-960- Domains for 1q2l:
Domain d1q2la1: 1q2l A:504-732 [118731]
complexed with pt, zn
Domain d1q2la2: 1q2l A:733-960 [118732]
complexed with pt, zn
Domain d1q2la3: 1q2l A:264-503 [118733]
complexed with pt, zn
Domain d1q2la4: 1q2l A:24-263 [118734]
complexed with pt, zn
- Domains for 1q2l:
More info for Protein Protease III from d.185.1.1: MPP-like
Timeline for Protein Protease III from d.185.1.1: MPP-like:
- Protein Protease III from d.185.1.1: MPP-like first appeared in SCOP 1.73
- Protein Protease III from d.185.1.1: MPP-like appears in SCOPe 2.06
- Protein Protease III from d.185.1.1: MPP-like appears in the current release, SCOPe 2.08