3h18

X-ray diffraction
2.4Å resolution

Crystal structure of EstE5-PMSF (II)

Released:

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Abhydrolase_3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 322 amino acids
Theoretical weight: 34.65 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q0GMU2 (Residues: 1-297; Coverage: 100%)
Gene name: estE5
Sequence domains: alpha/beta hydrolase fold
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: P41212
Unit cell:
a: 61.283Å b: 61.283Å c: 149.894Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.184 0.26
Expression system: Escherichia coli BL21(DE3)