GLIC mutant E75A. Determined by X-ray diffraction at 2.7 Å resolution. Released 10 Jan 2018.
Explore 6F13 in 3D Show helices and sheets RCSB PDB PDBe
6F13 contains 66 α-helices and 65 β-strands across 5 chains. 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 | 6-10 | 5 | |
| α-helix | 14-15 | 2 | |
| β-strand | 16-31 | 16 | 1 |
| β-strand | 36-48 | 13 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 56-59 | 4 | |
| β-strand | 64-65 | 2 | 1 |
| α-helix | 68-70 | 3 | |
| β-strand | 76-78 | 3 | 2 |
| β-strand | 81 | 1 | 1 |
| β-strand | 86-94 | 9 | 1 |
| β-strand | 99-111 | 13 | 1 |
| β-strand | 123-133 | 11 | 2 |
| β-strand | 140-144 | 5 | 1 |
| α-helix | 146-148 | 3 | |
| β-strand | 150-151 | 2 | 1 |
| β-strand | 157 | 1 | 2 |
| β-strand | 160-176 | 17 | 2 |
| β-strand | 179-192 | 14 | 2 |
| α-helix | 197 | 1 | |
| α-helix | 198-202 | 5 | |
| α-helix | 203-212 | 10 | |
| α-helix | 213-217 | 5 | |
| α-helix | 221-244 | 24 | |
| α-helix | 254-281 | 28 | |
| α-helix | 285-314 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-10 | 5 | |
| α-helix | 14-15 | 2 | |
| β-strand | 16-31 | 16 | 3 |
| β-strand | 36-48 | 13 | 3 |
| α-helix | 50-52 | 3 | |
| α-helix | 56-59 | 4 | |
| β-strand | 64-65 | 2 | 3 |
| α-helix | 68-70 | 3 | |
| β-strand | 76-78 | 3 | 4 |
| β-strand | 81 | 1 | 3 |
| β-strand | 86-94 | 9 | 3 |
| β-strand | 99-111 | 13 | 3 |
| α-helix | 116-118 | 3 | |
| β-strand | 123-133 | 11 | 4 |
| β-strand | 140-144 | 5 | 3 |
| α-helix | 146-148 | 3 | |
| β-strand | 150-151 | 2 | 3 |
| β-strand | 157 | 1 | 4 |
| β-strand | 160-176 | 17 | 4 |
| β-strand | 179-192 | 14 | 4 |
| α-helix | 197 | 1 | |
| α-helix | 198-202 | 5 | |
| α-helix | 203-212 | 10 | |
| α-helix | 213-217 | 5 | |
| α-helix | 221-244 | 24 | |
| α-helix | 254-281 | 28 | |
| α-helix | 285-314 | 30 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proton-gated ion channel | A, B, C, D, E | protein | 317 | Gloeobacter violaceus (strain PCC 7421) | Q7NDN8 (AlphaFold model) |
>6F13_1 Proton-gated ion channel (chains A, B, C, D, E) GQDMVSPPPPIADEPLTVNTGIYLIECYSLDDKAETFKVNAFLSLSWKDRRLAFDPVRSG VRVKTYEPEAIWIPAIRFVNVENARDADVVDISVSPDGTVQYLERFSARVLSPLDFRRYP FDSQTLHIYLIVRSVDTRNIVLAVDLEKVGKNDDVFLTGWDIESFTAVVKPANFALEDRL ESKLDYQLRISRQYFSYIPNIILPMLFILFISWTAFWSTSYEANVTLVVSTLIAHIAFNI LVETNLPKTPYMTYTGAIIFMIYLFYFVAVIEVTVQHYLKVESQPARAASITRASRIAFP VVFLLANIILAFLFFGF
| ID | Name | Formula | Copies |
|---|---|---|---|
| LMT | Dodecyl-beta-D-maltoside | C24 H46 O11 | 6 |
| PLC | Diundecyl phosphatidyl choline | C32 H65 N O8 P | 14 |
Water and common crystallization additives (NA, CL, ACT) are not listed.
Full mutational mapping of titratable residues helps to identify proton-sensors involved in the control of channel gating in the Gloeobacter violaceus pentameric ligand-gated ion channel. Nemecz, A., Hu, H., Fourati, Z. et al. PLoS Biol (2017) 15:e2004470-e2004470. DOI 10.1371/journal.pbio.2004470 · PubMed
Other PDB entries of the same protein (UniProt Q7NDN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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