› 1ffx

X-ray diffraction
3.95Å resolution

TUBULIN:STATHMIN-LIKE DOMAIN COMPLEX

Released:
DOI: 10.2210/pdb1ffx/pdb
PDB entry 1ffx coloured by chain, front view.
PDB entry 1ffx coloured by chain, side view.
PDB entry 1ffx coloured by chain, top view.
Source organisms:
Primary publication:
The 4 A X-ray structure of a tubulin:stathmin-like domain complex.
Gigant B, Curmi PA, Martin-Barbey C, Charbaut E, Lachkar S, Lebeau L, Siavoshian S, Sobel A, Knossow M
Cell 102 809-16 (2000)
PMID: 11030624

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
PDBe Complex ID:
PDB-CPX-526592 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Tubulin alpha-1A chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 451 amino acids
Theoretical weight: 50.12 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P02550 (Residues: 1-451; Coverage: 100%)
Gene name: TUBA1A
Sequence domains:
Structure domains:
Tubulin beta chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 445 amino acids
Theoretical weight: 49.91 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P02554 (Residues: 1-445; Coverage: 100%)
Sequence domains:
Structure domains:
PROTEIN (STATHMIN-LIKE DOMAIN OF RB3) Chain: E
Molecule details ›
Chain: E
Length: 91 amino acids
Theoretical weight: 7.76 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli

Ligands and Environments

2 bound ligands:
Ligand GTP 2 x GTP
Ligand GDP 2 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P65
Unit cell:
a: 328.5Å b: 328.5Å c: 54.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.267 0.267 0.367
Expression system: Escherichia coli

Quick links

Citations

39 review citations

Dynamics and mechanics of the microtubule plus end.
Howard et al. (2003)
38 more

14 mentions without citation

Molecular interactions at the colchicine binding site in tubulin: An X-ray crystallography perspective.
Wang et al. (2022)
13 more