› 3zu2

X-ray diffraction
2.1Å resolution

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (SIRAS)

Released:
DOI: 10.2210/pdb3zu2/pdb
PDB entry 3zu2 coloured by chain, front view.
PDB entry 3zu2 coloured by chain, side view.
PDB entry 3zu2 coloured by chain, top view.
Source organism: Yersinia pestis CO92
Primary publication:
Structure of the Yersinia pestis FabV enoyl-ACP reductase and its interaction with two 2-pyridone inhibitors.
Hirschbeck MW, Kuper J, Lu H, Liu N, Neckles C, Shah S, Wagner S, Sotriffer CA, Tonge PJ, Kisker C
Structure 20 89-100 (2012)
PMID: 22244758

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: 45.92 KDa
Source organism: Yersinia pestis CO92
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
1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1, ESRF BEAMLINE ID29
Spacegroup: P6522
Unit cell:
a: 104.16Å b: 104.16Å c: 219.14Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.199 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Bacterial lipids: metabolism and membrane homeostasis.
Parsons et al. (2013)
4 more

1 mention without citation

Structure of the Yersinia pestis FabV enoyl-ACP reductase and its interaction with two 2-pyridone inhibitors.
Hirschbeck et al. (2012)