2AWN
Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ATP-Mg)
Summary for 2AWN
Entry DOI | 10.2210/pdb2awn/pdb |
Related | 1Q12 1Q1B 1Q1E |
Descriptor | Maltose/maltodextrin import ATP-binding protein malK, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | atp-binding cassette, transport protein |
Biological source | Escherichia coli |
Cellular location | Cell inner membrane; Peripheral membrane protein: P68187 |
Total number of polymer chains | 4 |
Total formula weight | 170544.16 |
Authors | Lu, G.,Westbrooks, J.M.,Davidson, A.L.,Chen, J. (deposition date: 2005-09-01, release date: 2005-12-13, Last modification date: 2023-08-23) |
Primary citation | Lu, G.,Westbrooks, J.M.,Davidson, A.L.,Chen, J. ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation. Proc.Natl.Acad.Sci.Usa, 102:17969-17974, 2005 Cited by PubMed: 16326809DOI: 10.1073/pnas.0506039102 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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