4gwn

X-ray diffraction
3Å resolution

Crystal structure of human mature meprin 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 (5 distinct):
Meprin A subunit beta Chain: A
Molecule details ›
Chain: A
Length: 553 amino acids
Theoretical weight: 62.81 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q16820 (Residues: 62-614; Coverage: 81%)
Gene name: MEP1B
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6122
Unit cell:
a: 74.96Å b: 74.96Å c: 502.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.238
Expression system: Trichoplusia ni