7uai

Electron Microscopy
2.8Å resolution

Meprin alpha helix in complex with fetuin-B

Released:

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:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-172583 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (5 distinct):
Meprin A subunit alpha Chains: B, C, D, E
Molecule details ›
Chains: B, C, D, E
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:
Fetuin-B Chains: A, H
Molecule details ›
Chains: A, H
Length: 388 amino acids
Theoretical weight: 42.93 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9UGM5 (Residues: 1-382; Coverage: 100%)
Gene name: FETUB
Sequence domains: Cystatin domain

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA, FUC
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.8Å
Relevant EMDB volumes: EMD-26426
Expression systems:
  • Drosophila melanogaster
  • Homo sapiens