PDBe 3tpq

X-ray diffraction
3.45Å resolution

Crystal structure of wild-type MAL RPEL domain in complex with five G-actins

Released:
Primary publication:
Sensing actin dynamics: structural basis for G-actin-sensitive nuclear import of MAL.
Biochem. Biophys. Res. Commun. 414 373-8 (2011)
PMID: 21964294

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Actin, alpha skeletal muscle Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 375 amino acids
Theoretical weight: 41.86 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:
MAL Chain: M
Molecule details ›
Chain: M
Length: 117 amino acids
Theoretical weight: 13.75 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Structure domains: Cobalamin-dependent Methionine Synthase; domain 2

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P6522
Unit cell:
a: 180.737Å b: 180.737Å c: 382.279Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.224 0.273
Expression system: Escherichia coli