3HLN
Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds
Summary for 3HLN
Entry DOI | 10.2210/pdb3hln/pdb |
Descriptor | ATP-dependent Clp protease proteolytic subunit, CALCIUM ION (2 entities in total) |
Functional Keywords | disulfide bond, disordered equatorial loops, atp-binding, hydrolase, nucleotide-binding, protease, serine protease, stress response, zymogen |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A6G7 |
Total number of polymer chains | 28 |
Total formula weight | 605851.00 |
Authors | Kimber, M.S.,Yu, A.Y.H.,Borg, M.,Chan, H.S.,Houry, W.A. (deposition date: 2009-05-27, release date: 2010-07-28, Last modification date: 2023-09-06) |
Primary citation | Kimber, M.S.,Yu, A.Y.,Borg, M.,Leung, E.,Chan, H.S.,Houry, W.A. Structural and Theoretical Studies Indicate that the Cylindrical Protease ClpP Samples Extended and Compact Conformations. Structure, 18:798-808, 2010 Cited by PubMed: 20637416DOI: 10.1016/j.str.2010.04.008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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