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

  1. Root: SCOPe 2.06
  2. 2170735Class d: Alpha and beta proteins (a+b) [53931] (385 folds)
  3. 2237726Fold d.185: LuxS/MPP-like metallohydrolase [63410] (1 superfamily)
    core: beta-alpha-beta(2)-alpha(2); 2 layers: alpha/beta
  4. 2237727Superfamily d.185.1: LuxS/MPP-like metallohydrolase [63411] (3 families) (S)
    Share the same "active site motif" HxxEH located in the first core helix, but differ in one of the zinc-binding residues
  5. 2237728Family 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. 2237955Protein Protease III [143500] (1 species)
    duplication: comprises four domains of this fold
  7. 2237956Species 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. 2237957Domain d1q2la1: 1q2l A:504-732 [118731]
    complexed with pt, zn

Details for d1q2la1

PDB Entry: 1q2l (more details), 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: (download)

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

SCOPe Domain Coordinates for d1q2la1:

Click to download the PDB-style file with coordinates for d1q2la1.
(The format of our PDB-style files is described here.)

Timeline for d1q2la1: