3t1i

X-ray diffraction
3Å resolution

Crystal Structure of Human Mre11: Understanding Tumorigenic Mutations

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human Mre11: understanding tumorigenic mutations.
Structure 19 1591-602 (2011)
PMID: 22078559

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-156104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Double-strand break repair protein MRE11 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 431 amino acids
Theoretical weight: 49.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49959 (Residues: 1-411; Coverage: 58%)
Gene names: HNGS1, MRE11, MRE11A
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P212121
Unit cell:
a: 134.79Å b: 135.21Å c: 135.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.227 0.25
Expression system: Escherichia coli