› 6gf3

X-ray diffraction
2.4Å 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-237164 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
Tubulin alpha-1B chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 451 amino acids
Theoretical weight: 50.2 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P81947 (Residues: 1-451; Coverage: 100%)
Sequence domains:
Structure domains:
Tubulin beta-2B chain Chain: B
Molecule details ›
Chain: B
Length: 445 amino acids
Theoretical weight: 50 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q6B856 (Residues: 1-445; Coverage: 100%)
Gene name: TUBB2B
Sequence domains:
Structure domains:
Tubulin beta-2B chain Chain: D
Stathmin-4 Chain: E
Tubulin tyrosine ligase Chain: F

Ligands and Environments

8 bound ligands:
Ligand GTP 2 x GTP
Ligand MG 4 x MG
Ligand CA 2 x CA
Ligand GDP 2 x GDP
Ligand MES 2 x MES
Ligand EX5 1 x EX5
Ligand EDO 1 x EDO
Ligand ACP 1 x ACP
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 104.72Å b: 158.15Å c: 180.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.251
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Targeting mRNA processing as an anticancer strategy.
Desterro et al. (2020)
6 other articles

2 mentions without citation

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

PDB-REDO

The sliders below show the change in model quality between original PDB entry and the PDB-REDO entry

Model Geometry
 
 
Data not available
DNA/RNA Geometry
 
 
Data not available
Fit model/data
 
 
Data not available
PDB-REDO