SCOPe 2.08: Domain d1q2la1: 1q2l A:504-732

Lineage for d1q2la1 (1q2l A:504-732)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 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] (3 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] (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

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

7. 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

8. Domain d1q2la1: 1q2l A:504-732 [118731]
   complexed with pt, zn

Details for d1q2la1

PDB Entry: 1q2l, 2.2 Å

PDB Description: crystal structure of pitrilysin

PDB Compounds: (A:) Protease III

SCOPe Domain Sequences for d1q2la1:

Sequence; same for both SEQRES and ATOM records:

>d1q2la1 d.185.1.1 (A:504-732) Protease III {Escherichia coli [TaxId: 562]}
npyipddfsliksekkydhpelivdesnlrvvyapsryfasepkadvslilrnpkamdsa
rnqvmfalndylaglaldqlsnqasvggisfstnannglmvnangytqrlpqlfqalleg
yfsytatedqleqakswynqmmdsaekgkafeqaimpaqmlsqvpyfsrderrkilpsit
lkevlayrdalksgarpefmvignmteaqattlardvqkqlgadgsewc

Timeline for d1q2la1:

• d1q2la1 first appeared in SCOP 1.73
  
• d1q2la1 appears in SCOPe 2.07