1E3A
A slow processing precursor penicillin acylase from Escherichia coli
Summary for 1E3A
Entry DOI | 10.2210/pdb1e3a/pdb |
Related | 1AI4 1AI5 1AI6 1AI7 1AJN 1AJP 1AJQ 1PNK 1PNL 1PNM |
Descriptor | PENICILLIN AMIDASE ALPHA SUBUNIT, PENICILLIN AMIDASE BETA SUBUNIT, CALCIUM ION, ... (6 entities in total) |
Functional Keywords | antibiotic resistance, amidase, ntn-hydrolase, hydrolysis of penicillin g acylase |
Biological source | ESCHERICHIA COLI More |
Total number of polymer chains | 2 |
Total formula weight | 91910.20 |
Authors | Hewitt, L.,Kasche, V.,Lummer, K.,Lewis, R.J.,Murshudov, G.N.,Verma, C.S.,Dodson, G.G.,Wilson, K.S. (deposition date: 2000-06-07, release date: 2000-11-29, Last modification date: 2023-12-13) |
Primary citation | Hewitt, L.,Kasche, V.,Lummer, K.,Lewis, R.J.,Murshudov, G.N.,Verma, C.S.,Dodson, G.G.,Wilson, K.S. Structure of a Slow Processing Precursor Penicillin Acylase from Escherichia Coli Reveals the Linker Peptide Blocking the Active-Site Cleft J.Mol.Biol., 302:887-, 2000 Cited by PubMed: 10993730DOI: 10.1006/JMBI.2000.4105 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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