› 1p8z

X-ray diffraction
2.6Å resolution

Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156

Released:
DOI: 10.2210/pdb1p8z/pdb
PDB entry 1p8z coloured by chain, front view.
PDB entry 1p8z coloured by chain, side view.
PDB entry 1p8z coloured by chain, top view.
Source organisms:
Primary publication:
From the first to the second domain of gelsolin: a common path on the surface of actin?
Irobi E, Burtnick LD, Urosev D, Narayan K, Robinson RC
FEBS Lett 552 86-90 (2003)
PMID: 14527665

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-139014 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Gelsolin Chain: G
Molecule details ›
Chain: G
Length: 136 amino acids
Theoretical weight: 15.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06396 (Residues: 52-187; Coverage: 18%)
Gene name: GSN
Sequence domains: Gelsolin repeat
Structure domains: Severin
Actin, alpha skeletal muscle Chain: A
Molecule details ›
Chain: A
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

3 bound ligands:
Ligand CD 3 x CD
Ligand CA 1 x CA
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3112
Unit cell:
a: 114.22Å b: 114.22Å c: 93.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.263
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Gelsolin: the tail of a molecular gymnast.
Nag et al. (2013)
3 more

7 mentions without citation

Identification of transient hub proteins and the possible structural basis for their multiple interactions.
Higurashi et al. (2008)
6 more