› 3ktt

Electron Microscopy
4Å resolution

Atomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0 Angstrom cryo-EM map

Released:
DOI: 10.2210/pdb3ktt/pdb
PDB entry 3ktt coloured by chain, front view.
PDB entry 3ktt coloured by chain, side view.
PDB entry 3ktt coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
Cong Y, Baker ML, Jakana J, Woolford D, Miller EJ, Reissmann S, Kumar RN, Redding-Johanson AM, Batth TS, Mukhopadhyay A, Ludtke SJ, Frydman J, Chiu W
Proc Natl Acad Sci U S A 107 4967-72 (2010)
PMID: 20194787
Related structures: EMD-5148

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174899 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
T-complex protein 1 subunit beta Chain: B
Molecule details ›
Chain: B
Length: 513 amino acids
Theoretical weight: 55.11 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3ZBH0 (Residues: 14-526; Coverage: 96%)
Gene name: CCT2
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4Å
Relevant EMDB volumes: EMD-5148

Quick links

Citations

19 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
18 more

3 mentions without citation

The TRiCky Business of Protein Folding in Health and Disease.
Ghozlan et al. (2022)
2 more