1esg

X-ray diffraction
1.9Å resolution

RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.

Released:
Source organism: Bacillus amyloliquefaciens
Primary publication:
Structure of BamHI bound to nonspecific DNA: a model for DNA sliding.
Mol Cell 5 889-95 (2000)
PMID: 10882125

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-113765 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Type II restriction enzyme BamHI Chains: A, B
Molecule details ›
Chains: A, B
Length: 213 amino acids
Theoretical weight: 24.6 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23940 (Residues: 1-213; Coverage: 100%)
Gene name: bamHIR
Sequence domains: Restriction endonuclease BamHI
Structure domains: Restriction Endonuclease
DNA (5'-D(*TP*GP*GP*AP*TP*TP*CP*A)-3') Chain: C
Molecule details ›
Chain: C
Length: 8 nucleotides
Theoretical weight: 2.44 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided
DNA (5'-D(*TP*GP*AP*AP*TP*CP*CP*A)-3') Chain: D
Molecule details ›
Chain: D
Length: 8 nucleotides
Theoretical weight: 2.41 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 114.8Å b: 91.1Å c: 66.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.23
Expression systems:
  • Escherichia coli
  • Not provided