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 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 |
Domain d1q2la2: 1q2l A:733-960 [118732] complexed with pt, zn |
PDB Entry: 1q2l (more details), 2.2 Å
SCOPe Domain Sequences for d1q2la2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1q2la2 d.185.1.1 (A:733-960) Protease III {Escherichia coli [TaxId: 562]} rnkdvvvdkkqsvifekagnstdsalaavfvptgydeytssayssllgqivqpwfynqlr teeqlgyavfafpmsvgrqwgmgfllqsndkqpsflwerykaffptaeaklramkpdefa qiqqavitqmlqapqtlgeeasklskdfdrgnmrfdsrdkivaqiklltpqkladffhqa vvepqgmailsqisgsqngkaeyvhpegwkvwenvsalqqtmplmsek
Timeline for d1q2la2: