1E4D

Structure of OXA10 beta-lactamase at pH 8.3

Summary for 1E4D

• Entry DOI: 10.2210/pdb1e4d/pdb
• Related: 1E3U
• Descriptor: BETA-LACTAMASE OXA-10, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: beta-lactamase, antiobitic resistance
• Biological source: PSEUDOMONAS AERUGINOSA
• Total number of polymer chains: 4
• Total formula weight: 112178.59

Authors

Maveyraud, L.,Golemi, D.,Kotra, L.P.,Tranier, S.,Vakulenko, S.,Mobashery, S.,Samama, J.P. (deposition date: 2000-07-03, release date: 2001-01-12, Last modification date: 2023-12-13)

Primary citation

Maveyraud, L.,Golemi, D.,Kotra, L.P.,Tranier, S.,Vakulenko, S.,Mobashery, S.,Samama, J.P.
Insights Into Class D Beta-Lactamases are Revealed by the Crystal Structure of the Oxa10 Enzyme from Pseudomonas Aeruginosa
Structure, 8:1289-, 2000

PubMed Abstract: beta-lactam antibiotic therapies are commonly challenged by the hydrolytic activities of beta-lactamases in bacteria. These enzymes have been grouped into four classes: A, B, C, and D. Class B beta-lactamases are zinc dependent, and enzymes of classes A, C, and D are transiently acylated on a serine residue in the course of the turnover chemistry. While class A and C beta-lactamases have been extensively characterized by biochemical and structural methods, class D enzymes remain the least studied despite their increasing importance in the clinic.

PubMed: 11188693
DOI: 10.1016/S0969-2126(00)00534-7

Experimental method

X-RAY DIFFRACTION (1.8 Å)