› 4bkq

X-ray diffraction
2.3Å resolution

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

Released:
DOI: 10.2210/pdb4bkq/pdb
PDB entry 4bkq coloured by chain, front view.
PDB entry 4bkq coloured by chain, side view.
PDB entry 4bkq 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

Reaction catalysed: 
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187181 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 45.94 KDa
Source organism: Yersinia pestis A1122
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8Z9U1 (Residues: 1-399; Coverage: 100%)
Gene names: YPO4104, YP_4011, fabV, y4119
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAI 1 x NAI
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6522
Unit cell:
a: 102.628Å b: 102.628Å c: 214.913Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.23
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