5n4e

X-ray diffraction
2.9Å resolution

Prolyl oligopeptidase B from Galerina marginata bound to 35mer hydrolysis and macrocyclization substrate - H698A mutant

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-100362 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dual function macrocyclase-peptidase POPB Chains: A, B
Molecule details ›
Chains: A, B
Length: 765 amino acids
Theoretical weight: 85.64 KDa
Source organism: Galerina marginata
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: H2E7Q8 (Residues: 1-730; Coverage: 100%)
Gene names: GALMADRAFT_78538, POPB
Sequence domains:
Structure domains: alpha/beta hydrolase
Alpha-amanitin proprotein 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 35 amino acids
Theoretical weight: 3.85 KDa
Source organism: Galerina marginata
Expression system: Not provided
UniProt:
  • Canonical: A0A067SLB9 (Residues: 1-35; Coverage: 100%)
Gene names: AMA1-1, GALMADRAFT_1387421

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 99.18Å b: 115Å c: 141.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.249 0.295
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided