4bkr

X-ray diffraction
1.8Å resolution

Enoyl-ACP reductase from Yersinia pestis (wildtype, removed Histag) with cofactor NADH

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:
PUTATIVE REDUCTASE YPZ3_3519 Chain: A
Molecule details ›
Chain: A
Length: 406 amino acids
Theoretical weight: 44.2 KDa
Source organism: Yersinia pestis A1122
Expression system: Escherichia coli BL21(DE3)
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3121
Unit cell:
a: 102.59Å b: 102.59Å c: 84.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.216
Expression system: Escherichia coli BL21(DE3)