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4FPD

Deprotonation of D96 in bacteriorhodopsin opens the proton uptake pathway

Summary for 4FPD
Entry DOI10.2210/pdb4fpd/pdb
Related1FBK 1JV7 1KG8 1KG9 1KGB
DescriptorBacteriorhodopsin, RETINAL, CHLORIDE ION, ... (5 entities in total)
Functional Keywords7 helix, transmembrane, proton pump, ion transport, deprotonation, retinal binding, membrane, transport protein
Biological sourceHalobacterium sp. NRC-1
Total number of polymer chains1
Total formula weight33566.94
Authors
Wang, T.,Sessions, A.O.,Lunde, C.S.,Rouani, S.,Glaeser, R.M.,Facciotti, M.T.,Duan, Y. (deposition date: 2012-06-22, release date: 2013-02-27, Last modification date: 2023-09-13)
Primary citationWang, T.,Sessions, A.O.,Lunde, C.S.,Rouhani, S.,Glaeser, R.M.,Duan, Y.,Facciotti, M.T.
Deprotonation of d96 in bacteriorhodopsin opens the proton uptake pathway.
Structure, 21:290-297, 2013
Cited by
PubMed: 23394942
DOI: 10.1016/j.str.2012.12.018
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

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