1jhc

X-ray diffraction
2Å resolution

LEXA S119A C-TERMINAL TRYPTIC FRAGMENT

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
Hydrolysis of Ala(84)-|-Gly bond in repressor LexA.
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
LexA repressor Chain: A
Molecule details ›
Chain: A
Length: 137 amino acids
Theoretical weight: 15.18 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7C2 (Residues: 68-202; Coverage: 67%)
Gene names: JW4003, b4043, exrA, lexA, spr, tsl, umuA
Sequence domains: Peptidase S24-like
Structure domains: Umud Fragment, subunit A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 49.88Å b: 49.88Å c: 103.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.278
Expression system: Escherichia coli