› 4bkr

X-ray diffraction
1.8Å resolution

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

Released:
DOI: 10.2210/pdb4bkr/pdb
PDB entry 4bkr coloured by chain, front view.
PDB entry 4bkr coloured by chain, side view.
PDB entry 4bkr coloured by chain, top view.
Source organism: Yersinia pestis A1122
Primary publication:
Selectivity of Pyridone- and Diphenyl Ether-Based Inhibitors for the Yersinia pestis FabV Enoyl-ACP Reductase.
Neckles C, Pschibul A, Lai CT, Hirschbeck M, Kuper J, Davoodi S, Zou J, Liu N, Pan P, Shah S, Daryaee F, Bommineni GR, Lai C, Simmerling C, Kisker C, Tonge PJ
Biochemistry 55 2992-3006 (2016)
PMID: 27136302

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164321 (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

4 bound ligands:
Ligand NAI 1 x NAI
Ligand GOL 2 x GOL
Ligand DMS 1 x DMS
Ligand NA 1 x NA
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)

Quick links

Citations

2 review citations

A Review of Fatty Acid Biosynthesis Enzyme Inhibitors as Promising Antimicrobial Drugs.
Bibens et al. (2023)
1 more

1 mention without citation

Selectivity of Pyridone- and Diphenyl Ether-Based Inhibitors for the Yersinia pestis FabV Enoyl-ACP Reductase.
Neckles et al. (2016)