› 4zlx

X-ray diffraction
2.31Å resolution

N-terminal DNA binding domain of the antitoxin Phd from phage P1

Released:
DOI: 10.2210/pdb4zlx/pdb
PDB entry 4zlx coloured by chain, front view.
PDB entry 4zlx coloured by chain, side view.
PDB entry 4zlx coloured by chain, top view.
Source organism: Escherichia virus P1
Primary publication:
An intrinsically disordered entropic switch determines allostery in Phd-Doc regulation.
Garcia-Pino A, De Gieter S, Talavera A, De Greve H, Efremov RG, Loris R
Nat Chem Biol 12 490-6 (2016)
PMID: 27159580

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170311 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antitoxin phd Chains: A, B
Molecule details ›
Chains: A, B
Length: 53 amino acids
Theoretical weight: 6.17 KDa
Source organism: Escherichia virus P1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06253 (Residues: 1-45; Coverage: 62%)
Gene name: phd
Sequence domains: Antitoxin Phd_YefM, type II toxin-antitoxin system
Structure domains: YefM-like domain

Ligands and Environments

1 bound ligand:
Ligand ACT 5 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P61
Unit cell:
a: 42.94Å b: 42.94Å c: 100.18Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.179 0.245
Expression system: Escherichia coli BL21(DE3)

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Citations

6 review citations

Formation, physiology, ecology, evolution and clinical importance of bacterial persisters.
Van den Bergh et al. (2017)
5 more