7AHK
Crystal structure of the outward-facing state of the substrate-free Na+-only bound glutamate transporter homolog GltPh
Summary for 7AHK
Entry DOI | 10.2210/pdb7ahk/pdb |
Descriptor | Glutamate transporter homolog, SODIUM ION, octyl beta-D-glucopyranoside, ... (8 entities in total) |
Functional Keywords | glutamate transporter, aminoacid transport, homologue, membrane protein |
Biological source | Pyrococcus horikoshii |
Total number of polymer chains | 1 |
Total formula weight | 49564.28 |
Authors | Kovalev, K.,Alleva, C.,Astashkin, A.,Machtens, J.-P.,Fahlke, C.,Gordeliy, V. (deposition date: 2020-09-24, release date: 2020-11-18, Last modification date: 2024-01-31) |
Primary citation | Alleva, C.,Kovalev, K.,Astashkin, R.,Berndt, M.I.,Baeken, C.,Balandin, T.,Gordeliy, V.,Fahlke, C.,Machtens, J.P. Na + -dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters. Sci Adv, 6:-, 2020 Cited by PubMed: 33208356DOI: 10.1126/sciadv.aba9854 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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