› 5eyp

X-ray diffraction
1.9Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-112163 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Tubulin alpha chain Chain: A
Molecule details ›
Chain: A
Length: 451 amino acids
Theoretical weight: 50.2 KDa
Source organism: Ovis aries
UniProt:
  • Canonical: D0VWZ0 (Residues: 1-451; Coverage: 100%)
Sequence domains:
Structure domains:
Tubulin beta chain Chain: B
Molecule details ›
Chain: B
Length: 445 amino acids
Theoretical weight: 50 KDa
Source organism: Ovis aries
UniProt:
  • Canonical: D0VWY9 (Residues: 1-445; Coverage: 100%)
Sequence domains:
Structure domains:
DESIGNED ANKYRIN REPEAT PROTEIN (DARPIN) Chain: F
Molecule details ›
Chain: F
Length: 169 amino acids
Theoretical weight: 17.96 KDa
Source organism: synthetic construct
Expression system: Escherichia coli K-12
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

6 bound ligands:
Ligand GTP 1 x GTP
Ligand MG 1 x MG
Ligand SO4 3 x SO4
Ligand GOL 8 x GOL
Ligand GDP 1 x GDP
Ligand LOC 1 x LOC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 87.57Å b: 71.76Å c: 93.05Å
α: 90° β: 99.85° γ: 90°
R-values:
R R work R free
0.175 0.174 0.208
Expression system: Escherichia coli K-12

Quick links

Citations

2 review citations

Advances in targeted degradation of endogenous proteins.
Röth et al. (2019)
1 more

13 mentions without citation

Computational Approaches to the Rational Design of Tubulin-Targeting Agents.
Pérez-Peña et al. (2023)
12 more