2ATS
Dihydrodipicolinate synthase co-crystallised with (S)-lysine
Summary for 2ATS
Entry DOI | 10.2210/pdb2ats/pdb |
Related | 1dhp 1o5k 1s5t 1s5v 1s5w 1yxd |
Descriptor | dihydrodipicolinate synthase, POTASSIUM ION, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | dihydrodipicolinate synthase, dhdps, lysine, inhibition, lyase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A6L2 |
Total number of polymer chains | 2 |
Total formula weight | 63197.54 |
Authors | Devenish, S.R.A.,Dobson, R.C.J.,Jameson, G.B.,Gerrard, J.A. (deposition date: 2005-08-26, release date: 2006-09-19, Last modification date: 2024-03-13) |
Primary citation | Devenish, S.R.A.,Dobson, R.C.J.,Jameson, G.B.,Gerrard, J.A. The co-crystallisation of (S)-lysine-bound dihydrodipicolinate synthase from E. coli indicates that domain movements are not responsible for (S)-lysine inhibition To be published, |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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