› 2vyp

X-ray diffraction
2.35Å resolution

Rabbit-muscle G-actin in complex with myxobacterial rhizopodin

Released:
DOI: 10.2210/pdb2vyp/pdb
PDB entry 2vyp coloured by chain, front view.
PDB entry 2vyp coloured by chain, side view.
PDB entry 2vyp coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
The absolute configuration of rhizopodin and its inhibition of actin polymerization by dimerization.
Hagelueken G, Albrecht SC, Steinmetz H, Jansen R, Heinz DW, Kalesse M, Schubert WD
Angew Chem Int Ed Engl 48 595-8 (2009)
PMID: 19035596

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159302 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Actin, alpha skeletal muscle Chains: A, B
Molecule details ›
Chains: A, B
Length: 377 amino acids
Theoretical weight: 42.1 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ATP 2 x ATP
Ligand CA 4 x CA
Ligand RH9 1 x RH9
Ligand HEZ 3 x HEZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P21212
Unit cell:
a: 77.653Å b: 194.863Å c: 53.038Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.241

Quick links

Citations

10 review citations

Biosynthesis of polyketides by trans-AT polyketide synthases.
Helfrich et al. (2016)
9 more

3 mentions without citation

Actin structure and function.
Dominguez et al. (2011)
2 more