› 1aoa

X-ray diffraction
2.4Å resolution

N-TERMINAL ACTIN-CROSSLINKING DOMAIN FROM HUMAN FIMBRIN

Released:
DOI: 10.2210/pdb1aoa/pdb
PDB entry 1aoa coloured by chain, front view.
PDB entry 1aoa coloured by chain, side view.
PDB entry 1aoa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of an actin-crosslinking domain from human fimbrin.
Goldsmith SC, Pokala N, Shen W, Fedorov AA, Matsudaira P, Almo SC
Nat Struct Biol 4 708-12 (1997)
PMID: 9302997

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plastin-3 Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 30.53 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P13797 (Residues: 101-375; Coverage: 44%)
Gene name: PLS3
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 50.032Å b: 61.241Å c: 102.298Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.285

Quick links

Citations

14 review citations

Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues.
Bennett et al. (2001)
13 more

12 mentions without citation

Transcriptional regulation in Saccharomyces cerevisiae: transcription factor regulation and function, mechanisms of initiation, and roles of activators and coactivators.
Hahn et al. (2011)
11 more