Cryo-EM structure of nanodisc (PE:PS:PC) reconstituted GLIC at pH 2.5. Determined by electron microscopy at 2.65 Å resolution. Released 17 Apr 2024.
Explore 8JJ3 in 3D Show helices and sheets RCSB PDB PDBe
8JJ3 contains 67 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 | 7-10 | 4 | |
| 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 |
| β-strand | 76-78 | 3 | 2 |
| β-strand | 81 | 1 | 1 |
| β-strand | 86-94 | 9 | 1 |
| β-strand | 99-111 | 13 | 1 |
| α-helix | 119-121 | 3 | |
| β-strand | 123-133 | 11 | 2 |
| β-strand | 140-144 | 5 | 1 |
| β-strand | 150-151 | 2 | 1 |
| β-strand | 160-167 | 8 | 2 |
| α-helix | 171 | 1 | |
| β-strand | 172-176 | 5 | 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 | 221-242 | 22 | |
| α-helix | 247-248 | 2 | |
| α-helix | 254-281 | 28 | |
| α-helix | 285-315 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-10 | 4 | |
| α-helix | 15 | 1 | |
| β-strand | 16-31 | 16 | 5 |
| β-strand | 36-48 | 13 | 5 |
| α-helix | 50-52 | 3 | |
| α-helix | 56-59 | 4 | |
| β-strand | 64-65 | 2 | 5 |
| β-strand | 76-78 | 3 | 6 |
| β-strand | 81 | 1 | 5 |
| β-strand | 86-94 | 9 | 5 |
| β-strand | 99-111 | 13 | 5 |
| α-helix | 119-121 | 3 | |
| β-strand | 123-133 | 11 | 6 |
| β-strand | 140-144 | 5 | 5 |
| β-strand | 150-151 | 2 | 5 |
| β-strand | 160-167 | 8 | 6 |
| α-helix | 171 | 1 | |
| β-strand | 172-176 | 5 | 6 |
| β-strand | 179-192 | 14 | 6 |
| α-helix | 197 | 1 | |
| α-helix | 198-202 | 5 | |
| α-helix | 203-212 | 10 | |
| α-helix | 213-217 | 5 | |
| α-helix | 221-242 | 22 | |
| α-helix | 247-248 | 2 | |
| α-helix | 254-281 | 28 | |
| α-helix | 285-315 | 31 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proton-gated ion channel | A, B, C, D, E | protein | 312 | Gloeobacter violaceus | Q7NDN8 (AlphaFold model) |
>8JJ3_1 Proton-gated ion channel (chains A, B, C, D, E) VSPPPPIADEPLTVNTGIYLIECYSLDDKAETFKVNAFLSLSWKDRRLAFDPVRSGVRVK TYEPEAIWIPEIRFVNVENARDADVVDISVSPDGTVQYLERFSARVLSPLDFRRYPFDSQ TLHIYLIVRSVDTRNIVLAVDLEKVGKNDDVFLTGWDIESFTAVVKPANFALEDRLESKL DYQLRISRQYFSYIPNIILPMLFILFISWTAFWSTSYEANVTLVVSTLIAHIAFNILVET NLPKTPYMTYTGAIIFMIYLFYFVAVIEVTVQHYLKVESQPARAASITRASRIAFPVVFL LANIILAFLFFG
| ID | Name | Formula | Copies |
|---|---|---|---|
| PEE | 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine | C41 H78 N O8 P | 45 |
Water and common crystallization additives (CL) are not listed.
Cryo-EM structures of prokaryotic ligand-gated ion channel GLIC provide insights into gating in a lipid environment. Bharambe, N., Li, Z., Seiferth, D. et al. Nat Commun (2024) 15:2967-2967. DOI 10.1038/s41467-024-47370-w · 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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