Laser excitation effects on BR: Reprocessed Dark from Nogly et al. Determined by X-ray diffraction at 1.44 Å resolution. Released 22 Jan 2025.
Explore 9F9G in 3D Show helices and sheets RCSB PDB PDBe
9F9G contains 13 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-31 | 22 | |
| α-helix | 37-61 | 25 | |
| β-strand | 67-71 | 5 | 1 |
| β-strand | 74-78 | 5 | 1 |
| α-helix | 81-100 | 20 | |
| α-helix | 105-127 | 23 | |
| α-helix | 131-151 | 21 | |
| α-helix | 152-156 | 5 | |
| α-helix | 157-160 | 4 | |
| α-helix | 165-191 | 27 | |
| α-helix | 201-213 | 13 | |
| α-helix | 214-218 | 5 | |
| α-helix | 219-224 | 6 | |
| α-helix | 227-229 | 3 | |
| α-helix | 231-232 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bacteriorhodopsin | A | protein | 231 | Halobacterium salinarum | P02945 (AlphaFold model) |
>9F9G_1 Bacteriorhodopsin (chains A) ITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLG YGLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGL VGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMRPEVASTFKVLRNVTVVLWS AYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
| ID | Name | Formula | Copies |
|---|---|---|---|
| RET | Retinal | C20 H28 O | 1 |
| OLC | (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate | C21 H40 O4 | 5 |
| LI1 | 1-[2,6,10.14-tetramethyl-hexadecan-16-yl]-2-[2,10,14-trimethylhexadecan-16-yl]g… | C42 H86 O3 | 12 |
Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate. Bertrand, Q., Nogly, P., Nango, E. et al. Nat Commun (2024) 15:10278-10278. DOI 10.1038/s41467-024-54422-8 · PubMed
Other PDB entries of the same protein (UniProt P02945 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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