› 1nhi

X-ray diffraction
2Å resolution

Crystal structure of N-terminal 40KD MutL (LN40) complex with ADPnP and one potassium

Released:
DOI: 10.2210/pdb1nhi/pdb
PDB entry 1nhi coloured by chain, front view.
PDB entry 1nhi coloured by chain, side view.
PDB entry 1nhi coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Monovalent cation dependence and preference of GHKL ATPases and kinases.
Hu X, Machius M, Yang W
FEBS Lett 544 268-73 (2003)
PMID: 12782329

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA mismatch repair protein MutL Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 37.22 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P23367 (Residues: 1-331; Coverage: 54%)
Gene names: JW4128, b4170, mutL
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MG 1 x MG
Ligand K 1 x K
Ligand EDO 2 x EDO
Ligand ANP 1 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I222
Unit cell:
a: 61.897Å b: 71.415Å c: 190.342Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.229
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Role of Na+ and K+ in enzyme function.
Page et al. (2006)
4 more

5 mentions without citation

The role of monovalent cations in the ATPase reaction of DNA gyrase.
Hearnshaw et al. (2015)
4 more