Bacteriorhodopsin/lipid complex at 1.47 a resolution. Determined by X-ray diffraction at 1.47 Å resolution. Released 11 Sept 2002.
Explore 1M0L in 3D Show helices and sheets RCSB PDB PDBe
1M0L contains 10 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 | 10-30 | 21 | |
| 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 | 131-154 | 24 | |
| α-helix | 165-191 | 27 | |
| α-helix | 201-213 | 13 | |
| α-helix | 214-218 | 5 | |
| α-helix | 219-225 | 7 | |
| α-helix | 227-229 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bacteriorhodopsin | A | protein | 262 | Halobacterium salinarum | P02945 (AlphaFold model) |
>1M0L_1 BACTERIORHODOPSIN (chains A) MLELLPTAVEGVSQAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITT LVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGT ILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMRPEV ASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSR AIFGEAEAPEPSAGDGAAATSD
| ID | Name | Formula | Copies |
|---|---|---|---|
| RET | Retinal | C20 H28 O | 1 |
| SQU | 2,10,23-trimethyl-tetracosane | C27 H56 | 1 |
| LI1 | 1-[2,6,10.14-tetramethyl-hexadecan-16-yl]-2-[2,10,14-trimethylhexadecan-16-yl]g… | C42 H86 O3 | 13 |
Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal. Schobert, B., Cupp-Vickery, J., Hornak, V. et al. J Mol Biol (2002) 321:715-726. DOI 10.1016/S0022-2836(02)00681-2 · 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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