› 8sha

Electron Microscopy
3Å resolution

CCT-G beta 5 complex closed state 4

Released:
DOI: 10.2210/pdb8sha/pdb
PDB entry 8sha coloured by chain, front view.
PDB entry 8sha coloured by chain, side view.
PDB entry 8sha 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-40482

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):
Guanine nucleotide-binding protein subunit beta-5 Chain: N
Molecule details ›
Chain: N
Length: 395 amino acids
Theoretical weight: 43.62 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: O14775 (Residues: 1-395; Coverage: 100%)
Gene name: GNB5
Sequence domains: WD domain, G-beta repeat
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
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

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-40482

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