4gwm

X-ray diffraction
1.85Å resolution

Crystal structure of human promeprin beta

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His(5)-|-Leu-, -Leu(6)-|-Cys-, -Ala(14)-|-Leu- and -Cys(19)-|-Gly- bonds in insulin B chain.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (8 distinct):
Meprin A subunit beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 592 amino acids
Theoretical weight: 67.29 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q16820 (Residues: 23-614; Coverage: 87%)
Gene name: MEP1B
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer : NEW Components: NAG, FUC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P1
Unit cell:
a: 69.62Å b: 71.12Å c: 85.74Å
α: 74.87° β: 80.08° γ: 65.13°
R-values:
R R work R free
0.168 0.168 0.188
Expression system: Trichoplusia ni