› 1wrp

X-ray diffraction
2.2Å resolution

FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR

Released:
DOI: 10.2210/pdb1wrp/pdb
PDB entry 1wrp coloured by chain, front view.
PDB entry 1wrp coloured by chain, side view.
PDB entry 1wrp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Flexibility of the DNA-binding domains of trp repressor.
Lawson CL, Zhang RG, Schevitz RW, Otwinowski Z, Joachimiak A, Sigler PB
Proteins 3 18-31 (1988)
PMID: 3375234

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141677 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trp operon repressor Chain: R
Molecule details ›
Chain: R
Length: 107 amino acids
Theoretical weight: 12.24 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A881 (Residues: 2-108; Coverage: 99%)
Gene names: JW4356, b4393, rtrY, trpR
Sequence domains: Trp repressor protein
Structure domains: TrpR-like

Ligands and Environments

1 bound ligand:
Ligand TRP 1 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 50.6Å b: 50.6Å c: 73.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 not available not available
Expression system: Not provided

Quick links

Citations

9 review citations

Folding funnels and binding mechanisms.
Ma et al. (1999)
8 more

10 mentions without citation

Simultaneous prediction of protein folding and docking at high resolution.
Das et al. (2009)
9 more