› 7uaf

Electron Microscopy
2.4Å resolution

Human meprin alpha inhibitory complex with compound 10d (N~3~,N~3~-bis[(2H-1,3-benzodioxol-5-yl)methyl]-N-hydroxy-beta-alaninamide)

Released:
DOI: 10.2210/pdb7uaf/pdb
PDB entry 7uaf coloured by chain, front view.
PDB entry 7uaf coloured by chain, side view.
PDB entry 7uaf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor.
Bayly-Jones C, Lupton CJ, Fritz C, Venugopal H, Ramsbeck D, Wermann M, Jäger C, de Marco A, Schilling S, Schlenzig D, Whisstock JC
OpenAccess logo Nat Commun 13 6178 (2022)
PMID: 36261433
Related structures: EMD-26423

Function and Biology Details

Reaction catalysed: 
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172582 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Meprin A subunit alpha Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 587 amino acids
Theoretical weight: 67.29 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: Q16819 (Residues: 22-600; Coverage: 80%)
Gene name: MEP1A
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, FUC
Carbohydrate polymer
4 bound ligands:
Ligand M6X 4 x M6X
Ligand CA 8 x CA
Ligand ZN 4 x ZN
Ligand NAG 4 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.4Å
Relevant EMDB volumes: EMD-26423
Expression system: Drosophila melanogaster

Quick links

Citations

4 citation in other articles

Cryo-EM structure of influenza helical nucleocapsid reveals NP-NP and NP-RNA interactions as a model for the genome encapsidation.
Chenavier et al. (2023)
3 more