› 1rpe

X-ray diffraction
2.5Å resolution

THE PHAGE 434 OR2/R1-69 COMPLEX AT 2.5 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1rpe/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1rpe coloured by chain, front view.
PDB entry 1rpe coloured by chain, side view.
PDB entry 1rpe coloured by chain, top view.
Source organism: Phage 434
Primary publication:
The phage 434 OR2/R1-69 complex at 2.5 A resolution.
Shimon LJ, Harrison SC
J Mol Biol 232 826-38 (1993)
PMID: 8355273

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-114529 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Repressor protein CI Chains: L, R
Molecule details ›
Chains: L, R
Length: 69 amino acids
Theoretical weight: 7.56 KDa
Source organism: Phage 434
UniProt:
  • Canonical: P16117 (Residues: 2-70; Coverage: 73%)
Gene name: CI
Sequence domains: Helix-turn-helix
Structure domains: lambda repressor-like DNA-binding domains
DNA (5'-D(*TP*AP*TP*AP*CP*AP*AP*TP*GP*TP*AP*TP*CP*TP*TP*GP*T P*TP*TP*G)-3') Chain: B
Molecule details ›
Chain: B
Length: 20 nucleotides
Theoretical weight: 6.13 KDa
Source organism: Phage 434
Expression system: Not provided
DNA (5'-D(*AP*CP*AP*AP*AP*CP*AP*AP*GP*AP*TP*AP*CP*AP*TP*TP*G P*TP*AP*T)-3') Chain: A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ELLIOTT GX-13
Spacegroup: P212121
Unit cell:
a: 149.29Å b: 64.29Å c: 27.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Two distinct modes of protein-induced bending in DNA.
El Hassan et al. (1998)
1 more

6 mentions without citation

An overview of the structures of protein-DNA complexes.
Luscombe et al. (2000)
5 more