› 8sht

Electron Microscopy
3Å resolution

CCT G beta 5 complex closed state 14

Released:
DOI: 10.2210/pdb8sht/pdb
PDB entry 8sht coloured by chain, front view.
PDB entry 8sht coloured by chain, side view.
PDB entry 8sht coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller.
Wang S, Sass MI, Kwon Y, Ludlam WG, Smith TM, Carter EJ, Gladden NE, Riggi M, Iwasa JH, Willardson BM, Shen PS
Mol Cell (2023)
PMID: 37852256
Related structures: EMD-40494

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero octadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-232712 (preferred)
Entry contents:
10 distinct polypeptide molecules
Macromolecules (10 distinct):
T-complex protein 1 subunit alpha Chains: A, a
Molecule details ›
Chains: A, a
Length: 536 amino acids
Theoretical weight: 58.24 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P17987 (Residues: 2-537; Coverage: 96%)
Gene names: CCT1, CCTA, TCP1
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit beta Chains: B, b
Molecule details ›
Chains: B, b
Length: 526 amino acids
Theoretical weight: 56.49 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P78371 (Residues: 2-527; Coverage: 98%)
Gene names: 99D8.1, CCT2, CCTB
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit delta Chains: D, d
T-complex protein 1 subunit epsilon Chains: E, e
T-complex protein 1 subunit gamma Chains: G, g
T-complex protein 1 subunit eta Chains: H, h
T-complex protein 1 subunit theta Chains: Q, q
T-complex protein 1 subunit zeta Chains: Z, z
Phosducin-like protein Chain: P
Guanine nucleotide-binding protein subunit beta-5 Chain: N

Ligands and Environments

3 bound ligands:
Ligand ADP 16 x ADP
Ligand MG 16 x MG
Ligand AF3 16 x AF3
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3Å
Relevant EMDB volumes: EMD-40494

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