› 1pne

X-ray diffraction
2Å resolution

CRYSTALLIZATION AND STRUCTURE DETERMINATION OF BOVINE PROFILIN AT 2.0 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1pne/pdb
PDB entry 1pne coloured by chain, front view.
PDB entry 1pne coloured by chain, side view.
PDB entry 1pne coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystallization and structure determination of bovine profilin at 2.0 A resolution.
Cedergren-Zeppezauer ES, Goonesekere NC, Rozycki MD, Myslik JC, Dauter Z, Lindberg U, Schutt CE
J Mol Biol 240 459-75 (1994)
PMID: 8046751

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-135935 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Profilin-1 Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 14.97 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P02584 (Residues: 2-140; Coverage: 99%)
Gene name: PFN1
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: 69.15Å b: 34.59Å c: 52.49Å
α: 90° β: 92.56° γ: 90°
R-values:
R R work R free
0.165 0.165 not available
Expression system: Not provided

Quick links

Citations

10 review citations

The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains.
Kay et al. (2000)
9 more

16 mentions without citation

Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation.
Richardson et al. (2002)
15 more