Bacteriorhodopsin/lipid complex at 1.55 a resolution. Determined by X-ray diffraction at 1.55 Å resolution. Released 15 Sept 1999.
Explore 1C3W in 3D Show helices and sheets RCSB PDB PDBe
1C3W 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 | 37-62 | 26 | |
| β-strand | 66-71 | 6 | 1 |
| β-strand | 74-79 | 6 | 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 (ground state wild type "br") | A | protein | 222 | Halobacterium salinarum | P02945 (AlphaFold model) |
>1C3W_1 BACTERIORHODOPSIN (GROUND STATE WILD TYPE "BR") (chains A) TGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGY GLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLV GALTKVYSYRFVWWAISTAAMLYILYVLFFGFSMRPEVASTFKVLRNVTVVLWSAYPVVW LIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFG
| ID | Name | Formula | Copies |
|---|---|---|---|
| LI1 | 1-[2,6,10.14-tetramethyl-hexadecan-16-yl]-2-[2,10,14-trimethylhexadecan-16-yl]g… | C42 H86 O3 | 13 |
| SQU | 2,10,23-trimethyl-tetracosane | C27 H56 | 1 |
| RET | Retinal | C20 H28 O | 1 |
Structure of bacteriorhodopsin at 1.55 A resolution. Luecke, H., Schobert, B., Richter, H.T. et al. J Mol Biol (1999) 291:899-911. DOI 10.1006/jmbi.1999.3027 · PubMed
Other PDB entries of the same protein (UniProt P02945 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1C3W is part of these collections:
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