3amj

X-ray diffraction
3Å resolution

The crystal structure of the heterodimer of M16B peptidase from Sphingomonas sp. A1

Released:

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123438 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Zinc peptidase inactive subunit Chains: B, D
Molecule details ›
Chains: B, D
Length: 424 amino acids
Theoretical weight: 45.9 KDa
Source organism: Sphingomonas sp. A1
Expression system: Escherichia coli
UniProt:
  • Canonical: F2Z283 (Residues: 1-424; Coverage: 100%)
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
Zinc peptidase active subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 437 amino acids
Theoretical weight: 48.4 KDa
Source organism: Sphingomonas sp. A1
Expression system: Escherichia coli
UniProt:
  • Canonical: F2Z284 (Residues: 1-437; Coverage: 100%)
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 67.457Å b: 100.676Å c: 253.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.21 0.3
Expression system: Escherichia coli