› 3zqh

X-ray diffraction
1.6Å resolution

Structure of Tetracycline repressor in complex with inducer peptide- TIP3

Released:
DOI: 10.2210/pdb3zqh/pdb
PDB entry 3zqh coloured by chain, front view.
PDB entry 3zqh coloured by chain, side view.
PDB entry 3zqh coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
An exclusive α/β code directs allostery in TetR-peptide complexes.
Sevvana M, Goetz C, Goeke D, Wimmer C, Berens C, Hillen W, Muller YA
J Mol Biol 416 46-56 (2012)
PMID: 22178479

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137868 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tetracycline repressor protein class B from transposon Tn10; Tetracycline repressor protein class D Chain: A
Molecule details ›
Chain: A
Length: 208 amino acids
Theoretical weight: 23.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04483 (Residues: 1-120, 122-187; Coverage: 90%)
  • Canonical: P0ACT4 (Residues: 121-121, 188-208; Coverage: 10%)
Gene name: tetR
Sequence domains:
Structure domains:
INDUCER PEPTIDE TIP3 Chain: C
Molecule details ›
Chain: C
Length: 15 amino acids
Theoretical weight: 1.85 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 73.35Å b: 57.34Å c: 57.81Å
α: 90° β: 112.29° γ: 90°
R-values:
R R work R free
0.183 0.18 0.224
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

1 review citation

The TetR family of regulators.
Cuthbertson et al. (2013)
9 other articles

1 mention without citation

Benchmarking of different molecular docking methods for protein-peptide docking.
Agrawal et al. (2019)