1qsd

X-ray diffraction
2.2Å resolution

RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p.
Nat Struct Biol 6 1029-32 (1999)
PMID: 10542094

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-155771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tubulin-specific chaperone A Chains: A, B
Molecule details ›
Chains: A, B
Length: 106 amino acids
Theoretical weight: 12.4 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P48606 (Residues: 1-106; Coverage: 100%)
Gene names: RBL2, YOR265W
Sequence domains: Tubulin binding cofactor A
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 45.4Å b: 110.1Å c: 49.4Å
α: 90° β: 106.2° γ: 90°
R-values:
R R work R free
0.211 0.208 0.297