› 3wrp

X-ray diffraction
1.8Å resolution

FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR

Released:
DOI: 10.2210/pdb3wrp/pdb
PDB entry 3wrp coloured by chain, front view.
PDB entry 3wrp coloured by chain, side view.
PDB entry 3wrp 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-532177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trp operon repressor Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 12.37 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A881 (Residues: 1-108; Coverage: 100%)
Gene names: JW4356, b4393, rtrY, trpR
Sequence domains: Trp repressor protein
Structure domains: TrpR-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 57.4Å b: 34.2Å c: 44.5Å
α: 90° β: 90° γ: 90°
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

8 mentions without citation

Development of a polarizable force field for proteins via ab initio quantum chemistry: first generation model and gas phase tests.
Kaminski et al. (2002)
7 more