6PM6: Zebra fish alpha-1 glycine receptor
CryoEM structure of zebra fish alpha-1 glycine receptor bound with Glycine in SMA, open state. Determined by electron microscopy at 2.9 Å resolution. Released 10 Feb 2021.
- Method
- Electron microscopy
- Resolution
- 2.9 Å
- Organism
- Danio rerio
- Chains
- 5
- Atoms
- 14,100
- Mol. weight
- 266 kDa
- Ligands
- GLY
- Released
- 10 Feb 2021
Explore 6PM6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6PM6 contains 76 α-helices and 75 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.
Chain A: 15 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-34 | 9 | |
| α-helix | 37-39 | 3 | |
| α-helix | 52 | 1 | |
| β-strand | 53-68 | 16 | 1 |
| β-strand | 73-85 | 13 | 1 |
| α-helix | 87-89 | 3 | |
| β-strand | 98-100 | 3 | 1 |
| α-helix | 105-107 | 3 | |
| β-strand | 114-116 | 3 | 2 |
| β-strand | 122-123 | 2 | 1 |
| β-strand | 132-137 | 6 | 1 |
| β-strand | 141-153 | 13 | 1 |
| α-helix | 161-163 | 3 | |
| β-strand | 165-174 | 10 | 2 |
| β-strand | 182-186 | 5 | 1 |
| β-strand | 192-194 | 3 | 1 |
| β-strand | 203-205 | 3 | 2 |
| β-strand | 211-213 | 3 | 2 |
| β-strand | 216-217 | 2 | 3 |
| β-strand | 222-223 | 2 | 3 |
| β-strand | 225-234 | 10 | 2 |
| α-helix | 239 | 1 | |
| α-helix | 240-244 | 5 | |
| α-helix | 245-247 | 3 | |
| α-helix | 249-256 | 8 | |
| α-helix | 267-285 | 19 | |
| α-helix | 300-303 | 4 | |
| α-helix | 305-324 | 20 | |
| α-helix | 394-405 | 12 | |
| α-helix | 410-426 | 17 | |
Chain B: 16 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-34 | 9 | |
| α-helix | 37-39 | 3 | |
| α-helix | 52 | 1 | |
| β-strand | 53-68 | 16 | 7 |
| β-strand | 73-85 | 13 | 7 |
| α-helix | 87-89 | 3 | |
| β-strand | 98-100 | 3 | 7 |
| α-helix | 105-107 | 3 | |
| β-strand | 114-116 | 3 | 8 |
| β-strand | 122-124 | 3 | 7 |
| β-strand | 132-137 | 6 | 7 |
| β-strand | 141-153 | 13 | 7 |
| α-helix | 161-163 | 3 | |
| β-strand | 165-174 | 10 | 8 |
| β-strand | 182-186 | 5 | 7 |
| β-strand | 192-194 | 3 | 7 |
| β-strand | 203-205 | 3 | 8 |
| β-strand | 211-213 | 3 | 8 |
| β-strand | 216-217 | 2 | 9 |
| β-strand | 222-223 | 2 | 9 |
| β-strand | 225-234 | 10 | 8 |
| α-helix | 236-238 | 3 | |
| α-helix | 239 | 1 | |
| α-helix | 240-244 | 5 | |
| α-helix | 245-247 | 3 | |
| α-helix | 249-256 | 8 | |
| α-helix | 267-285 | 19 | |
| α-helix | 300-303 | 4 | |
| α-helix | 305-324 | 20 | |
| α-helix | 392-405 | 14 | |
| α-helix | 410-426 | 17 | |
Chain C: 15 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-34 | 9 | |
| α-helix | 37-39 | 3 | |
| α-helix | 52 | 1 | |
| β-strand | 53-68 | 16 | 10 |
| β-strand | 73-85 | 13 | 10 |
| α-helix | 87-89 | 3 | |
| β-strand | 98-100 | 3 | 10 |
| α-helix | 105-107 | 3 | |
| β-strand | 114-116 | 3 | 11 |
| β-strand | 122-124 | 3 | 10 |
| β-strand | 132-137 | 6 | 10 |
| β-strand | 141-153 | 13 | 10 |
| α-helix | 161-163 | 3 | |
| β-strand | 165-174 | 10 | 11 |
| β-strand | 182-186 | 5 | 10 |
| β-strand | 192-194 | 3 | 10 |
| β-strand | 203-205 | 3 | 11 |
| β-strand | 211-213 | 3 | 11 |
| β-strand | 216-217 | 2 | 12 |
| β-strand | 222-223 | 2 | 12 |
| β-strand | 225-234 | 10 | 11 |
| α-helix | 239 | 1 | |
| α-helix | 240-244 | 5 | |
| α-helix | 245-247 | 3 | |
| α-helix | 249-256 | 8 | |
| α-helix | 267-285 | 19 | |
| α-helix | 300-303 | 4 | |
| α-helix | 305-324 | 20 | |
| α-helix | 392-405 | 14 | |
| α-helix | 410-426 | 17 | |
Chain D: 15 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-34 | 9 | |
| α-helix | 37-39 | 3 | |
| α-helix | 52 | 1 | |
| β-strand | 53-68 | 16 | 4 |
| β-strand | 73-85 | 13 | 4 |
| α-helix | 87-89 | 3 | |
| β-strand | 98-100 | 3 | 4 |
| α-helix | 105-107 | 3 | |
| β-strand | 114-116 | 3 | 5 |
| β-strand | 122-124 | 3 | 4 |
| β-strand | 132-137 | 6 | 4 |
| β-strand | 141-153 | 13 | 4 |
| α-helix | 161-163 | 3 | |
| β-strand | 165-174 | 10 | 5 |
| β-strand | 182-186 | 5 | 4 |
| β-strand | 192-194 | 3 | 4 |
| β-strand | 203-205 | 3 | 5 |
| β-strand | 211-213 | 3 | 5 |
| β-strand | 216-217 | 2 | 6 |
| β-strand | 222-223 | 2 | 6 |
| β-strand | 225-234 | 10 | 5 |
| α-helix | 237-239 | 3 | |
| α-helix | 240-244 | 5 | |
| α-helix | 245-247 | 3 | |
| α-helix | 249-256 | 8 | |
| α-helix | 267-285 | 19 | |
| α-helix | 300-303 | 4 | |
| α-helix | 305-324 | 20 | |
| α-helix | 391-405 | 15 | |
| α-helix | 410-426 | 17 | |
Chain E: 15 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-34 | 9 | |
| α-helix | 37-39 | 3 | |
| α-helix | 52 | 1 | |
| β-strand | 53-68 | 16 | 13 |
| β-strand | 73-85 | 13 | 13 |
| α-helix | 87-89 | 3 | |
| β-strand | 98-100 | 3 | 13 |
| α-helix | 105-107 | 3 | |
| β-strand | 114-116 | 3 | 14 |
| β-strand | 122-124 | 3 | 13 |
| β-strand | 132-137 | 6 | 13 |
| β-strand | 141-153 | 13 | 13 |
| α-helix | 161-163 | 3 | |
| β-strand | 165-174 | 10 | 14 |
| β-strand | 182-186 | 5 | 13 |
| β-strand | 192-194 | 3 | 13 |
| β-strand | 203-205 | 3 | 14 |
| β-strand | 211-213 | 3 | 14 |
| β-strand | 216-217 | 2 | 15 |
| β-strand | 222-223 | 2 | 15 |
| β-strand | 225-234 | 10 | 14 |
| α-helix | 239 | 1 | |
| α-helix | 240-244 | 5 | |
| α-helix | 245-247 | 3 | |
| α-helix | 249-256 | 8 | |
| α-helix | 266-285 | 20 | |
| α-helix | 300-303 | 4 | |
| α-helix | 305-324 | 20 | |
| α-helix | 392-405 | 14 | |
| α-helix | 410-426 | 17 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Glycine receptor subunit alphaZ1 | A, B, C, D, E | protein | 458 | Danio rerio | O93430 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>6PM6_1 Glycine receptor subunit alphaZ1 (chains A, B, C, D, E)
MFALGIYLWETIVFFSLAASQQAAARKAASPMPPSEFLDKLMGKVSGYDARIRPNFKGPP
VNVTCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPSMLDSIWKP
DLFFANEKGANFHEVTTDNKLLRISKNGNVLYSIRITLVLACPMDLKNFPMDVQTCIMQL
ESFGYTMNDLIFEWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHL
ERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPK
VSYVKAIDIWMAVCLLFVFSALLEYAAVNFIARQHKELLRFQRRRRHLKEDEAGDGRFSF
AAYGMGPACLQAKDGMAIKGNNNNAPTSTNPPEKTVEEMRKLFISRAKRIDTVSRVAFPL
VFLIFNIFYWITYKIIRSEDIHKQLVPRGSHHHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| GLY | Glycine | C2 H5 N O2 | 5 |
Primary citation
Mechanism of gating and partial agonist action in the glycine receptor. Yu, J., Zhu, H., Lape, R. et al. Cell (2021) 184:957-968.e21. DOI 10.1016/j.cell.2021.01.026 · PubMed
Other PDB entries of the same protein (UniProt O93430 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7M6N 2.61 Å, Full length alpha1 Glycine receptor in presence of 0.1mM Glycine
- 7U2N 2.8 Å, A novel compound mimics the structural and functional effects of the full agonist…
- 7M6O 2.84 Å, Full length alpha1 Glycine receptor in presence of 0.1mM Glycine and 32uM…
- 6PLX 2.9 Å, CryoEM structure of zebra fish alpha-1 glycine receptor bound with GABA in SMA,…
- 6PLY 2.9 Å, CryoEM structure of zebra fish alpha-1 glycine receptor bound with GABA in SMA, open state
- 6PXD 2.9 Å, CryoEM structure of zebra fish alpha-1 glycine receptor, Apo state
- 7U2M 2.9 Å, A novel compound mimics the structural and functional effects of the full agonist…
- 7M6Q 2.91 Å, Full length alpha1 Glycine receptor in presence of 1mM Glycine and 32uM…
- 6PLS 3.0 Å, CryoEM structure of zebra fish alpha-1 glycine receptor bound with taurine in nanodisc,…
- 6PLW 3.0 Å, CryoEM structure of zebra fish alpha-1 glycine receptor bound with GABA in SMA,…
- 6PLZ 3.0 Å, CryoEM structure of zebra fish alpha-1 glycine receptor bound with GABA in SMA, closed…
- 6PM1 3.0 Å, CryoEM structure of zebra fish alpha-1 glycine receptor bound with Taurine in SMA,…
Browse structure collections
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