› 4b1v

X-ray diffraction
1.75Å resolution

Structure of the Phactr1 RPEL-N domain bound to G-actin

Released:
DOI: 10.2210/pdb4b1v/pdb
PDB entry 4b1v coloured by chain, front view.
PDB entry 4b1v coloured by chain, side view.
PDB entry 4b1v coloured by chain, top view.
Source organisms:
Primary publication:
Structures of the Phactr1 RPEL domain and RPEL motif complexes with G-actin reveal the molecular basis for actin binding cooperativity.
Mouilleron S, Wiezlak M, O'Reilly N, Treisman R, McDonald NQ
Structure 20 1960-70 (2012)
PMID: 23041370

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159304 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Actin, alpha skeletal muscle Chains: A, B
Molecule details ›
Chains: A, B
Length: 376 amino acids
Theoretical weight: 41.97 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 2-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:
Phosphatase and actin regulator 1 Chains: M, N
Molecule details ›
Chains: M, N
Length: 32 amino acids
Theoretical weight: 3.84 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q2M3X8 (Residues: 133-164; Coverage: 6%)
Gene name: Phactr1
Sequence domains: RPEL repeat

Ligands and Environments

5 bound ligands:
Ligand EDO 4 x EDO
Ligand ATP 2 x ATP
Ligand LAB 2 x LAB
Ligand MG 2 x MG
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 44.121Å b: 75.924Å c: 122.451Å
α: 90° β: 97.01° γ: 90°
R-values:
R R work R free
0.182 0.18 0.221
Expression system: Not provided

Quick links

Citations

4 review citations

Guardians of the actin monomer.
Xue et al. (2013)
3 more