› 4b2t

X-ray diffraction
5.5Å resolution

The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning

Released:
DOI: 10.2210/pdb4b2t/pdb
PDB entry 4b2t coloured by chain, front view.
PDB entry 4b2t coloured by chain, side view.
PDB entry 4b2t coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning.
Kalisman N, Schröder GF, Levitt M
Structure 21 540-9 (2013)
PMID: 23478063

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123315 (preferred)
Entry contents:
8 distinct polypeptide molecules
Macromolecules (8 distinct):
T-complex protein 1 subunit alpha Chains: A, a
Molecule details ›
Chains: A, a
Length: 556 amino acids
Theoretical weight: 60.28 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q32L40 (Residues: 1-556; Coverage: 100%)
Gene names: CCT1, TCP1
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit beta Chains: B, b
Molecule details ›
Chains: B, b
Length: 535 amino acids
Theoretical weight: 57.56 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3ZBH0 (Residues: 1-535; Coverage: 100%)
Gene name: CCT2
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit delta Chains: D, d
Molecule details ›
Chains: D, d
Length: 542 amino acids
Theoretical weight: 58.23 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q2T9X2 (Residues: 1-542; Coverage: 100%)
Gene name: CCT4
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit epsilon Chains: E, e
Molecule details ›
Chains: E, e
Length: 541 amino acids
Theoretical weight: 59.7 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: F1MWD3 (Residues: 1-541; Coverage: 100%)
Gene name: CCT5
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit gamma Chains: G, g
Molecule details ›
Chains: G, g
Length: 545 amino acids
Theoretical weight: 60.67 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3T0K2 (Residues: 1-545; Coverage: 100%)
Gene name: CCT3
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit eta Chains: H, h
Molecule details ›
Chains: H, h
Length: 543 amino acids
Theoretical weight: 59.52 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q2NKZ1 (Residues: 1-543; Coverage: 100%)
Gene name: CCT7
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit theta Chains: Q, q
Molecule details ›
Chains: Q, q
Length: 548 amino acids
Theoretical weight: 59.68 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3ZCI9 (Residues: 1-548; Coverage: 100%)
Gene name: CCT8
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit zeta Chains: Z, z
Molecule details ›
Chains: Z, z
Length: 531 amino acids
Theoretical weight: 58.04 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3MHL7 (Residues: 1-531; Coverage: 100%)
Gene name: CCT6A
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 272.7Å b: 313.5Å c: 158.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.34 0.34 0.399

Quick links

Citations

9 review citations

In vivo aspects of protein folding and quality control.
Balchin et al. (2016)
8 more

5 mentions without citation

The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning.
Kalisman et al. (2013)
4 more