X-ray diffraction
2.5Å resolution

Ternary complex of the WH2 domain of mim with actin-dnase I


Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Actin, alpha skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 41.88 KDa
Source organism: Oryctolagus cuniculus
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:
Deoxyribonuclease-1 Chain: B
Molecule details ›
Chain: B
Length: 260 amino acids
Theoretical weight: 29.09 KDa
Source organism: Bos taurus
  • Canonical: P00639 (Residues: 23-282; Coverage: 100%)
Gene names: DNASE1, DNL1
Sequence domains: Endonuclease/Exonuclease/phosphatase family
Structure domains: Endonuclease/exonuclease/phosphatase
Protein MTSS 1 Chain: C
Molecule details ›
Chain: C
Length: 32 amino acids
Theoretical weight: 3.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: O43312 (Residues: 724-755; Coverage: 4%)
Gene names: KIAA0429, MIM, MTSS1
Sequence domains: WH2 motif

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 42.093Å b: 75.487Å c: 228.991Å
α: 90° β: 90° γ: 90°
R R work R free
0.22 0.217 0.284
Expression system: Not provided