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2ATS

Dihydrodipicolinate synthase co-crystallised with (S)-lysine

Summary for 2ATS
Entry DOI10.2210/pdb2ats/pdb
Related1dhp 1o5k 1s5t 1s5v 1s5w 1yxd
Descriptordihydrodipicolinate synthase, POTASSIUM ION, CHLORIDE ION, ... (5 entities in total)
Functional Keywordsdihydrodipicolinate synthase, dhdps, lysine, inhibition, lyase
Biological sourceEscherichia coli
Cellular locationCytoplasm: P0A6L2
Total number of polymer chains2
Total formula weight63197.54
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 citationDevenish, 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

227111

數據於2024-11-06公開中

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