CryoEM structure of zebra fish alpha-1 glycine receptor bound with GABA in SMA, open state. Determined by electron microscopy at 2.9 Å resolution. Released 6 Jan 2021.
Explore 6PLY in 3D Show helices and sheets RCSB PDB PDBe
6PLY contains 69 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-34 | 9 | |
| 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 | 103-108 | 6 | |
| β-strand | 114-116 | 3 | 2 |
| β-strand | 122-124 | 3 | 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 | 239-242 | 4 | |
| α-helix | 249-254 | 6 | |
| α-helix | 256-258 | 3 | |
| α-helix | 268-285 | 18 | |
| α-helix | 300-303 | 4 | |
| α-helix | 308-323 | 16 | |
| α-helix | 393-396 | 4 | |
| α-helix | 401-404 | 4 | |
| α-helix | 410-427 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-34 | 9 | |
| 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 | 103-108 | 6 | |
| 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 | 239-242 | 4 | |
| α-helix | 249-254 | 6 | |
| α-helix | 256-258 | 3 | |
| α-helix | 268-285 | 18 | |
| α-helix | 308-323 | 16 | |
| α-helix | 393-396 | 4 | |
| α-helix | 401-404 | 4 | |
| α-helix | 410-427 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-34 | 9 | |
| 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 | 103-108 | 6 | |
| 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 | 239-242 | 4 | |
| α-helix | 245-254 | 10 | |
| α-helix | 256-258 | 3 | |
| α-helix | 268-285 | 18 | |
| α-helix | 300-303 | 4 | |
| α-helix | 308-323 | 16 | |
| α-helix | 393-396 | 4 | |
| α-helix | 401-404 | 4 | |
| α-helix | 410-427 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycine receptor subunit alphaZ1 | A, B, C, D, E | protein | 458 | Danio rerio | O93430 (AlphaFold model) |
>6PLY_1 Glycine receptor subunit alphaZ1 (chains A, B, C, D, E) MFALGIYLWETIVFFSLAASQQAAARKAASPMPPSEFLDKLMGKVSGYDARIRPNFKGPP VNVTCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPSMLDSIWKP DLFFANEKGANFHEVTTDNKLLRISKNGNVLYSIRITLVLACPMDLKNFPMDVQTCIMQL ESFGYTMNDLIFEWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHL ERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPK VSYVKAIDIWMAVCLLFVFSALLEYAAVNFIARQHKELLRFQRRRRHLKEDEAGDGRFSF AAYGMGPACLQAKDGMAIKGNNNNAPTSTNPPEKTVEEMRKLFISRAKRIDTVSRVAFPL VFLIFNIFYWITYKIIRSEDIHKQLVPRGSHHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| ABU | Gamma-amino-butanoic acid | C4 H9 N O2 | 5 |
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:
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