› 1ut5

X-ray diffraction
2.75Å resolution

Divalent metal ions (manganese) bound to T5 5'-exonuclease

Released:
DOI: 10.2210/pdb1ut5/pdb
PDB entry 1ut5 coloured by chain, front view.
PDB entry 1ut5 coloured by chain, side view.
PDB entry 1ut5 coloured by chain, top view.
Source organism: Escherichia virus T5
Primary publication:
Roles of divalent metal ions in flap endonuclease-substrate interactions.
Feng M, Patel D, Dervan JJ, Ceska T, Suck D, Haq I, Sayers JR
Nat Struct Mol Biol 11 450-6 (2004)
PMID: 15077103

Function and Biology Details

Reaction catalysed: 
Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flap endonuclease Chains: A, B
Molecule details ›
Chains: A, B
Length: 291 amino acids
Theoretical weight: 33.49 KDa
Source organism: Escherichia virus T5
Expression system: Escherichia coli
UniProt:
  • Canonical: P06229 (Residues: 1-291; Coverage: 100%)
Gene names: D15, T5.130, T5p128, exo5
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MN 3 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43
Unit cell:
a: 77.6Å b: 77.6Å c: 134.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.252 0.334
Expression system: Escherichia coli

Quick links

Citations

5 review citations

One is enough: insights into the two-metal ion nuclease mechanism from global analysis and computational studies.
Dupureur CM. (2010)
4 more

6 mentions without citation

Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases.
Grasby et al. (2012)
5 more