a5b3 GABAA Receptor resting state. Determined by electron microscopy at 3.14 Å resolution. Released 12 Nov 2025.
Explore 9HAA in 3D Show helices and sheets RCSB PDB PDBe
9HAA contains 64 α-helices and 64 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 | 10-23 | 14 | |
| β-strand | 41-56 | 16 | 1 |
| β-strand | 61-73 | 13 | 1 |
| α-helix | 75-77 | 3 | |
| β-strand | 85-88 | 4 | 1 |
| α-helix | 90-93 | 4 | |
| β-strand | 102-103 | 2 | 2 |
| β-strand | 106-111 | 6 | 1 |
| β-strand | 119-124 | 6 | 1 |
| β-strand | 128-140 | 13 | 1 |
| α-helix | 148-150 | 3 | |
| β-strand | 152-160 | 9 | 2 |
| β-strand | 169-173 | 5 | 1 |
| α-helix | 177-180 | 4 | |
| β-strand | 182-183 | 2 | 1 |
| β-strand | 188 | 1 | 1 |
| β-strand | 193-207 | 15 | 2 |
| β-strand | 210-223 | 14 | 2 |
| α-helix | 226-228 | 3 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-245 | 12 | |
| α-helix | 246-248 | 3 | |
| α-helix | 254-278 | 25 | |
| α-helix | 287-315 | 29 | |
| α-helix | 324-350 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-20 | 13 | |
| α-helix | 35 | 1 | |
| β-strand | 36-51 | 16 | 3 |
| β-strand | 56-68 | 13 | 3 |
| α-helix | 70-72 | 3 | |
| β-strand | 82-83 | 2 | 3 |
| α-helix | 85-90 | 6 | |
| β-strand | 96-98 | 3 | 4 |
| β-strand | 101-106 | 6 | 3 |
| β-strand | 114-118 | 5 | 3 |
| β-strand | 123-135 | 13 | 3 |
| α-helix | 140-142 | 3 | |
| β-strand | 147-156 | 10 | 4 |
| β-strand | 164-168 | 5 | 3 |
| α-helix | 171-173 | 3 | |
| β-strand | 175-176 | 2 | 3 |
| α-helix | 178-180 | 3 | |
| β-strand | 186-200 | 15 | 4 |
| β-strand | 203-216 | 14 | 4 |
| α-helix | 219-221 | 3 | |
| α-helix | 222-226 | 5 | |
| α-helix | 227-237 | 11 | |
| α-helix | 238-241 | 4 | |
| α-helix | 247-271 | 25 | |
| α-helix | 280-307 | 28 | |
| α-helix | 550-581 | 32 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-20 | 12 | |
| α-helix | 35 | 1 | |
| β-strand | 36-51 | 16 | 5 |
| β-strand | 56-68 | 13 | 5 |
| α-helix | 70-72 | 3 | |
| β-strand | 81-83 | 3 | 5 |
| α-helix | 85-89 | 5 | |
| β-strand | 96-98 | 3 | 6 |
| β-strand | 101-106 | 6 | 5 |
| β-strand | 114-118 | 5 | 5 |
| β-strand | 123-135 | 13 | 5 |
| α-helix | 140-145 | 6 | |
| β-strand | 147-156 | 10 | 6 |
| β-strand | 164-168 | 5 | 5 |
| α-helix | 171-173 | 3 | |
| β-strand | 175-176 | 2 | 5 |
| α-helix | 178-180 | 3 | |
| β-strand | 186-200 | 15 | 6 |
| β-strand | 203-216 | 14 | 6 |
| α-helix | 219-221 | 3 | |
| α-helix | 222-226 | 5 | |
| α-helix | 227-236 | 10 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-269 | 23 | |
| α-helix | 280-307 | 28 | |
| α-helix | 550-583 | 34 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-25 | 11 | |
| β-strand | 41-56 | 16 | 7 |
| β-strand | 61-73 | 13 | 7 |
| α-helix | 75-77 | 3 | |
| β-strand | 85-87 | 3 | 7 |
| α-helix | 90-93 | 4 | |
| β-strand | 101-103 | 3 | 8 |
| β-strand | 106-111 | 6 | 7 |
| β-strand | 113 | 1 | 9 |
| β-strand | 117 | 1 | 9 |
| β-strand | 119-124 | 6 | 7 |
| β-strand | 128-140 | 13 | 7 |
| α-helix | 145-150 | 6 | |
| β-strand | 152-161 | 10 | 8 |
| β-strand | 169-173 | 5 | 7 |
| β-strand | 181-183 | 3 | 7 |
| β-strand | 188 | 1 | 7 |
| β-strand | 193-207 | 15 | 8 |
| β-strand | 210-223 | 14 | 8 |
| α-helix | 226-228 | 3 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-241 | 8 | |
| α-helix | 245-248 | 4 | |
| α-helix | 254-275 | 22 | |
| α-helix | 287-314 | 28 | |
| α-helix | 325-349 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-20 | 13 | |
| α-helix | 35 | 1 | |
| β-strand | 36-51 | 16 | 10 |
| β-strand | 56-68 | 13 | 10 |
| α-helix | 70-72 | 3 | |
| β-strand | 82-83 | 2 | 10 |
| α-helix | 85-90 | 6 | |
| β-strand | 96-98 | 3 | 11 |
| β-strand | 101-106 | 6 | 10 |
| β-strand | 114-118 | 5 | 10 |
| β-strand | 123-135 | 13 | 10 |
| α-helix | 140-142 | 3 | |
| β-strand | 147-156 | 10 | 11 |
| β-strand | 164-168 | 5 | 10 |
| α-helix | 171-173 | 3 | |
| β-strand | 175-176 | 2 | 10 |
| β-strand | 186-199 | 14 | 11 |
| β-strand | 204-216 | 13 | 11 |
| α-helix | 219-221 | 3 | |
| α-helix | 222-226 | 5 | |
| α-helix | 227-236 | 10 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-271 | 25 | |
| α-helix | 280-306 | 27 | |
| α-helix | 553-583 | 31 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Green fluorescent protein,Gamma-aminobutyric acid receptor subunit alpha-5 | A, D | protein | 679 | Aequorea victoria, Homo sapiens | P31644 (AlphaFold model), P42212 (AlphaFold model) |
| Gamma-aminobutyric acid receptor subunit beta-3,Green fluorescent protein | B, C, E | protein | 623 | Homo sapiens, Aequorea victoria | P28472 (AlphaFold model), P42212 (AlphaFold model) |
>9HAA_1 Green fluorescent protein,Gamma-aminobutyric acid receptor subunit alpha-5 (chains A, D) MRKSPGLSDCLWAWILLLSTLTGRSYGQMSKGEELFTGVVPILVELDGDVNGHKFSVRGE GEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGY VQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYI TADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPN EKRDHMVLLEFVTAAGITHGMDELYKAANALAAWSHPQFEKGGGSGGGSGGGSWSHPQFE KSSSNNNNNENLYFQAMPTSSVKDETNDNITIFTRILDGLLDGYDNRLRPGLGERITQVR TDIYVTSFGPVSDTEMEYTIDVFFRQSWKDERLRFKGPMQRLPLNNLLASKIWTPDTFFH NGKKSIAHNMTTPNKLLRLEDDGTLLYTMRLTISAECPMQLEDFPMDAHACPLKFGSYAY PNSEVVYVWTNGSTKSVVVAEDGSRLNQYHLMGQTVGTENISTSTGEYTIMTAHFHLKRK IGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAY ATAMDWFIAVCYAFVFSALIEFATVNYFTKSQPARAASISKIDKMSRIVFPVLFGTFNLV YWATYLNREPVIKGAASPK
>9HAA_2 Gamma-aminobutyric acid receptor subunit beta-3,Green fluorescent protein (chains B, C, E) MWGLAGGRLFGIFSAPVLVAVVCCAQSVNDPGNMSFVKETVDKLLKGYDIRLRPDFGGPP VCVGMNIDIASIDMVSEVNMDYTLTMYFQQYWRDKRLAYSGIPLNLTLDNRVADQLWVPD TYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIE SYGYTTDDIEFYWRGGDKAVTGVERIELPQFSIVEHRLVSRNVVFATGAYPRLSLSFRLK RNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKI PYVKAIDMYLMGCFVFVFLALLEYAFVNYIFFSQPGRAMVSKGEELFTGVVPILVEMDGD VNGRKFSVRGVGEGDATHGKLTLKFICTSGKLPVPWPTLVTTLSYGVQCFSRYPDHMKQH DFFKSAMPEGYVQERTIFFKDDGSYKTRAEVKFEGDTLVNRIVLKGTDFKEDGNILGHKL EYNMNVGNVYITADKQKNGIKANFEIRHNVEDGGVQLADHYQQNTPIGDGSVLLPDNHYL SVQVKLSKDPNEKRDHMVLLEFRTAAGITPGMDELYKGRAAAIDRWSRIVFPFTFSLFNL VYWLYYVNSRENLYFQAHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| BUA | butanoic acid | C4 H8 O2 | 2 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (EPE) are not listed.
Structural basis for activation and potentiation in a human alpha 5 beta 3 GABA A receptor. Cowgill, J., Fan, C., Steyaert, J. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-74279-3 · PubMed
Other PDB entries of the same protein (UniProt P31644 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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