› 1acf

X-ray diffraction
2Å resolution

ACANTHAMOEBA CASTELLANII PROFILIN IB

Released:
DOI: 10.2210/pdb1acf/pdb
PDB entry 1acf coloured by chain, front view.
PDB entry 1acf coloured by chain, side view.
PDB entry 1acf coloured by chain, top view.
Source organism: Acanthamoeba castellanii
Primary publication:
X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.
Fedorov AA, Magnus KA, Graupe MH, Lattman EE, Pollard TD, Almo SC
Proc Natl Acad Sci U S A 91 8636-40 (1994)
PMID: 8078936

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Profilin-1B Chain: A
Molecule details ›
Chain: A
Length: 125 amino acids
Theoretical weight: 12.85 KDa
Source organism: Acanthamoeba castellanii
Expression system: Not provided
UniProt:
  • Canonical: Q95VF7 (Residues: 2-126; Coverage: 99%)
Sequence domains: Profilin
Structure domains: Dynein light chain 2a, cytoplasmic

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 110.031Å b: 31.631Å c: 33.487Å
α: 90° β: 111.38° γ: 90°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Not provided

Quick links

Citations

6 review citations

The role of profilin complexes in cell motility and other cellular processes.
Witke W. (2004)
5 more

17 mentions without citation

An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state.
Zhang et al. (2004)
16 more