1K5Q
PENICILLIN ACYLASE, MUTANT COMPLEXED WITH PAA
Summary for 1K5Q
Entry DOI | 10.2210/pdb1k5q/pdb |
Related | 1AI4 1AI5 1AI6 1AI7 1JX9 1fxv 1pnk 1pnl |
Descriptor | PENICILLIN G ACYLASE ALPHA SUBUNIT, PENICILLIN G ACYLASE BETA SUBUNIT, CALCIUM ION, ... (5 entities in total) |
Functional Keywords | ntn-hydrolase fold, helices, beta-strands, hydrolase |
Biological source | Escherichia coli More |
Total number of polymer chains | 2 |
Total formula weight | 86382.47 |
Authors | Hensgens, C.M.H.,Keizer, E.,Snijder, H.J.,Dijkstra, B.W. (deposition date: 2001-10-12, release date: 2003-09-02, Last modification date: 2024-03-13) |
Primary citation | Alkema, W.B.L.,Hensgens, C.M.H.,Snijder, H.J.,Keizer, E.,Dijkstra, B.W.,Janssen, D.B. Structural and kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase. Protein Eng.Des.Sel., 17:473-480, 2004 Cited by PubMed: 15254299DOI: 10.1093/protein/gzh057 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.34 Å) |
Structure validation
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