1HDH

Arylsulfatase from Pseudomonas aeruginosa

Summary for 1HDH

• Entry DOI: 10.2210/pdb1hdh/pdb
• Descriptor: Arylsulfatase, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: hydrolase, sulfatase, formylglycine hydrate
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 120887.74

Authors

Boltes, I.,Czapinska, H.,Kahnert, A.,von Buelow, R.,Dirks, T.,Schmidt, B.,von Figura, K.,Kertesz, M.A.,Uson, I. (deposition date: 2000-11-16, release date: 2001-11-15, Last modification date: 2024-10-16)

Primary citation

Boltes, I.,Czapinska, H.,Kahnert, A.,von Buelow, R.,Dirks, T.,Schmidt, B.,von Figura, K.,Kertesz, M.A.,Uson, I.
1.3 A Structure of Arylsulfatase from Pseudomonas Aeruginosa Establishes the Catalytic Mechanism of Sulfate Ester Cleavage in the Sulfatase Family.
Structure, 9:483-491, 2001

PubMed Abstract: Sulfatases constitute a family of enzymes with a highly conserved active site region including a Calpha-formylglycine that is posttranslationally generated by the oxidation of a conserved cysteine or serine residue. The crystal structures of two human arylsulfatases, ASA and ASB, along with ASA mutants and their complexes led to different proposals for the catalytic mechanism in the hydrolysis of sulfate esters.

PubMed: 11435113
DOI: 10.1016/S0969-2126(01)00609-8

Experimental method

X-RAY DIFFRACTION (1.3 Å)