› 6o5n

X-ray diffraction
3Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-236991 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Tubulin alpha-1B chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 450 amino acids
Theoretical weight: 50.04 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: Q2XVP4 (Residues: 1-450; Coverage: 100%)
Gene name: TUBA1B
Sequence domains:
Tubulin beta chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 445 amino acids
Theoretical weight: 50 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P02554 (Residues: 1-445; Coverage: 100%)
Sequence domains:
Stathmin-4 Chain: E
Molecule details ›
Chain: E
Length: 143 amino acids
Theoretical weight: 16.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H169 (Residues: 49-189; Coverage: 75%)
Gene name: STMN4
Sequence domains: Stathmin family
Tubulin Tyrosine Ligase Chain: F
Molecule details ›
Chain: F
Length: 384 amino acids
Theoretical weight: 44.38 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli

Ligands and Environments

6 bound ligands:
Ligand GTP 2 x GTP
Ligand MG 3 x MG
Ligand CA 2 x CA
Ligand GDP 2 x GDP
Ligand MES 2 x MES
Ligand QW9 2 x QW9
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 105.301Å b: 157.764Å c: 182.084Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.202 0.245
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Colchicine-Binding Site Inhibitors from Chemistry to Clinic: A Review.
McLoughlin et al. (2020)
5 more

2 mentions without citation

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