› 3j3x

Electron Microscopy
4.3Å resolution

Independent reconstruction of Mm-cpn cryo-EM density map from half dataset in the closed state (training map)

Released:
DOI: 10.2210/pdb3j3x/pdb
PDB entry 3j3x coloured by chain, front view.
PDB entry 3j3x coloured by chain, side view.
PDB entry 3j3x coloured by chain, top view.
Source organism: Methanococcus maripaludis
Primary publication:
Cryo-EM model validation using independent map reconstructions.
DiMaio F, Zhang J, Chiu W, Baker D
Protein Sci 22 865-8 (2013)
PMID: 23592445
Related structures: EMD-5645

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183295 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 532 amino acids
Theoretical weight: 57.21 KDa
Source organism: Methanococcus maripaludis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q877G8 (Residues: 1-532; Coverage: 98%)
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.3Å
Relevant EMDB volumes: EMD-5645
Expression system: Escherichia coli

Quick links

Citations

9 review citations

How cryo-EM is revolutionizing structural biology.
Bai et al. (2015)
8 more

3 mentions without citation

Cryo-EM model validation using independent map reconstructions.
DiMaio et al. (2013)
2 more