X-ray diffraction
1.77Å resolution

Crystal structure of the lanthipeptide zinc-metallopeptidase EryP mutant E802R from saccharopolyspora erythraea

Entry authors: Zhao C, Zhao NL, Bao R

Function and Biology Details

Reaction catalysed:
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Aminopeptidase N Chain: A
Molecule details ›
Chain: A
Length: 884 amino acids
Theoretical weight: 98.26 KDa
Source organism: Saccharopolyspora erythraea NRRL 2338
Expression system: Escherichia coli BL21(DE3)
  • Canonical: A4F9D7 (Residues: 2-860; Coverage: 100%)
Gene names: A8924_1736, SACE_1339
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21
Unit cell:
a: 58.909Å b: 143.583Å c: 60.58Å
α: 90° β: 114.76° γ: 90°
R R work R free
0.14 0.139 0.171
Expression system: Escherichia coli BL21(DE3)