SCOP 1.73: Domain d1q2la3: 1q2l A:264-503

Lineage for d1q2la3 (1q2l A:264-503)

1. Root: SCOP 1.73

2. Class d: Alpha and beta proteins (a+b) [53931] (334 folds)

3. Fold d.185: LuxS/MPP-like metallohydrolase [63410] (1 superfamily)
   core: beta-alpha-beta(2)-alpha(2); 2 layers: alpha/beta

4. Superfamily d.185.1: LuxS/MPP-like metallohydrolase [63411] (2 families)
   Share the same "active site motif" HxxEH located in the first core helix, but differ in one of the zinc-binding residues

5. Family d.185.1.1: MPP-like [63412] (6 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

6. Protein Protease III [143500] (1 species)
   duplication: comprises four domains of this fold

7. Species Escherichia coli [TaxId:562] [143501] (1 PDB entry)

8. Domain d1q2la3: 1q2l A:264-503 [118733]
   complexed with pt, zn

Details for d1q2la3

PDB Entry: 1q2l, 2.2 Å

PDB Description: crystal structure of pitrilysin

PDB Compounds: (A:) Protease III

SCOP Domain Sequences for d1q2la3:

Sequence; same for both SEQRES and ATOM records:

>d1q2la3 d.185.1.1 (A:264-503) Protease III {Escherichia coli [TaxId: 562]}
eitvpvvtdaqkgiiihyvpalprkvlrvefridnnsakfrsktdelitylignrspgtl
sdwlqkqglvegisansdpivngnsgvlaisasltdkglanrdqvvaaifsylnllrekg
idkqyfdelanvldidfrypsitrdmdyvewladtmirvpvehtldavniadrydakavk
erlammtpqnariwyispkephnktayfvdapyqvdkisaqtfadwqkkaadialslpel

Timeline for d1q2la3:

• d1q2la3 is new in SCOP 1.73
  
• d1q2la3 appears in SCOP 1.75
  
• d1q2la3 appears in the current release, SCOPe 2.08