› 6nyy

Electron Microscopy
3Å resolution

human m-AAA protease AFG3L2, substrate-bound

Released:
DOI: 10.2210/pdb6nyy/pdb
PDB entry 6nyy coloured by chain, front view.
PDB entry 6nyy coloured by chain, side view.
PDB entry 6nyy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.
Puchades C, Ding B, Song A, Wiseman RL, Lander GC, Glynn SE
Mol Cell 75 1073-1085.e6 (2019)
PMID: 31327635
Related structures: EMD-0552

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-167170 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mitochondrial inner membrane m-AAA protease component AFG3L2 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 529 amino acids
Theoretical weight: 58.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y4W6 (Residues: 272-797; Coverage: 66%)
Gene name: AFG3L2
Sequence domains:
Substrate Chains: G, H, I, J
Molecule details ›
Chains: G, H, I, J
Length: 11 amino acids
Theoretical weight: 800 Da
Source organism: Homo sapiens
Expression system: Escherichia coli

Ligands and Environments

4 bound ligands:
Ligand ZN 6 x ZN
Ligand ANP 3 x ANP
Ligand MG 3 x MG
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3Å
Relevant EMDB volumes: EMD-0552
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Quality control of the mitochondrial proteome.
Song et al. (2021)
9 more

8 mentions without citation

The molecular principles governing the activity and functional diversity of AAA+ proteins.
Puchades et al. (2020)
7 more