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Literature summary extracted from

  • Bochtler, M.; Odintsov, S.G.; Marcyjaniak, M.; Sabala, I.
    Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases (2004), Protein Sci., 13, 854-861.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.16.4 Zn2+ tetrahedrally coordinated by two histidines, an aspartate, and a water molecule Streptomyces albus
3.4.24.75 Zn2+ the central Zn2+ is tetrahedrally coordinated by two histidines, an aspartate, and a water molecule. The Zn2+ chelating residue occur in the order histidine, aspartate, histidine and contact the metal via the Nepsilon, the Odelta and the Ndelta respectively, H210(Nepsilon), D214(Odelta), H293(Ndelta) Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.4 Streptomyces albus
-
-
-
3.4.24.75 Staphylococcus aureus
-
-
-

Synonyms

EC Number Synonyms Comment Organism
3.4.16.4 D-Ala-D-Ala carboxypeptidase
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 Streptomyces albus