Glycine receptor subunit alpha-2
Homo sapiens
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count | Chain A; UniProt 1–452 Chain B; UniProt 1–452 Chain C; UniProt 1–452 Chain D; UniProt 1–452 Chain E; UniProt 1–452 | Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 GLY GLYCINE × 5 | ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE | Resolution 3.55 Å |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
| Other PDB | Difference from Current Entry 9Y7X | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 5BKF Cyro-EM structure of human Glycine Receptor alpha2-beta heteromer, Glycine bound, desensitized state Deposited 2021-03-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Insufficient information Heteromer;Protein × 5 PDB declaration: pentameric |
Chain A
28–343(316 aa)
Chain A
409–452(44 aa)
Chain B
28–343(316 aa)
Chain B
409–452(44 aa)
Chain C
28–343(316 aa)
Chain C
409–452(44 aa)
Chain D
28–343(316 aa)
Chain D
409–452(44 aa)
|
Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 GLY GLYCINE × 5 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.60 Å |
| 5BKG Cyro-EM structure of human Glycine Receptor alpha2-beta heteromer, glycine bound, (semi)open state Deposited 2021-03-19 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Insufficient information Heteromer;Protein × 5 PDB declaration: pentameric |
Chain A
28–343(316 aa)
Chain A
409–452(44 aa)
Chain B
28–343(316 aa)
Chain B
409–452(44 aa)
Chain C
28–343(316 aa)
Chain C
409–452(44 aa)
Chain D
28–343(316 aa)
Chain D
409–452(44 aa)
|
Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 GLY GLYCINE × 3 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 7KUY Cyro-EM structure of human Glycine Receptor alpha2-beta heteromer, strychnine bound state Deposited 2020-11-25 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Insufficient information Heteromer;Protein × 5 PDB declaration: pentameric |
Chain A
28–343(316 aa)
Chain A
409–452(44 aa)
Chain B
28–343(316 aa)
Chain B
409–452(44 aa)
Chain C
28–343(316 aa)
Chain C
409–452(44 aa)
Chain D
28–343(316 aa)
Chain D
409–452(44 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 SY9 STRYCHNINE × 5 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.60 Å |
| 7L31 Cyro-EM structure of human Glycine Receptor alpha2-beta heteromer, strychnine bound state, 3.8 Angstrom Deposited 2020-12-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Insufficient information Heteromer;Protein × 5 PDB declaration: pentameric |
Chain A
28–343(316 aa)
Chain A
409–452(44 aa)
Chain B
28–343(316 aa)
Chain B
409–452(44 aa)
Chain C
28–343(316 aa)
Chain C
409–452(44 aa)
Chain D
28–343(316 aa)
Chain D
409–452(44 aa)
|
Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted Mutation:second cytoplasmic domain deleted | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 SY9 STRYCHNINE × 5 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 9Y7P Homomeric Glycine Receptor alpha2 with 1 mM Glycine in a Desensitized State Deposited 2025-09-11 | Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 5 PDB declaration: pentameric |
Chain A
1–452(452 aa)
Chain B
1–452(452 aa)
Chain C
1–452(452 aa)
Chain D
1–452(452 aa)
Chain E
1–452(452 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 GLY GLYCINE × 5 PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 30 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.50 Å |
| 9Y7W Homomeric Glycine Receptor alpha2 with 1 mM Glycine in an Open State Deposited 2025-09-11 | Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 5 PDB declaration: pentameric |
Chain A
1–452(452 aa)
Chain B
1–452(452 aa)
Chain C
1–452(452 aa)
Chain D
1–452(452 aa)
Chain E
1–452(452 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 GLY GLYCINE × 5 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.19 Å |
| 9Y7Z Homomeric Glycine Receptor alpha2 with 0.1 mM Glycine in a Desensitized State Deposited 2025-09-11 | Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 5 PDB declaration: pentameric |
Chain A
1–452(452 aa)
Chain B
1–452(452 aa)
Chain C
1–452(452 aa)
Chain D
1–452(452 aa)
Chain E
1–452(452 aa)
|
Not recorded | PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 GLY GLYCINE × 5 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.78 Å |
| 9Y80 Homomeric Glycine Receptor alpha2 with PTX in a Desensitized State Deposited 2025-09-11 | Different ligand/ion | Assembly 1 Protein homooligomer Homooligomer;Protein × 5 PDB declaration: pentameric |
Chain A
1–452(452 aa)
Chain B
1–452(452 aa)
Chain C
1–452(452 aa)
Chain D
1–452(452 aa)
Chain E
1–452(452 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 GLY GLYCINE × 5 RI5 (1aR,2aR,3S,6R,6aS,8aS,8bR,9R)-2a-hydroxy-8b-methyl-9-(prop-1-en-2-yl)hexahydro-3,6-methano-1,5,7-trioxacyclopenta[ij]c yclopropa[a]azulene-4,8(3H)-dione × 1 PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 15 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.55 Å |
| 9Y8Z Homomeric Glycine Receptor alpha2 with 0.1 mM Glycine in an Apo State Deposited 2025-09-11 | Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 5 PDB declaration: pentameric |
Chain A
1–452(452 aa)
Chain B
1–452(452 aa)
Chain C
1–452(452 aa)
Chain D
1–452(452 aa)
Chain E
1–452(452 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 30 CLR CHOLESTEROL × 5 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.50 Å |
| 9Y94 Homomeric Glycine Receptor alpha2 with PTX in an Open State Deposited 2025-09-13 | Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 5 PDB declaration: pentameric |
Chain A
1–452(452 aa)
Chain B
1–452(452 aa)
Chain C
1–452(452 aa)
Chain D
1–452(452 aa)
Chain E
1–452(452 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 GLY GLYCINE × 5 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.60 Å |
| 9Y95 Homomeric Glycine Receptor alpha2 with PTX in an Apo State Deposited 2025-09-13 | Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 5 PDB declaration: pentameric |
Chain A
1–452(452 aa)
Chain B
1–452(452 aa)
Chain C
1–452(452 aa)
Chain D
1–452(452 aa)
Chain E
1–452(452 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 20 RI5 (1aR,2aR,3S,6R,6aS,8aS,8bR,9R)-2a-hydroxy-8b-methyl-9-(prop-1-en-2-yl)hexahydro-3,6-methano-1,5,7-trioxacyclopenta[ij]c yclopropa[a]azulene-4,8(3H)-dione × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.45 Å |
| 9Y96 Homomeric Glycine Receptor alpha2 with 1 mM Glycine in a Closed State Deposited 2025-09-13 | Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 5 PDB declaration: pentameric |
Chain A
1–452(452 aa)
Chain B
1–452(452 aa)
Chain C
1–452(452 aa)
Chain D
1–452(452 aa)
Chain E
1–452(452 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 GLY GLYCINE × 5 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.36 Å |
12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | GLRA2_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–452; UniProt 1–452 Author chain B; PDBConstruct 1–452; UniProt 1–452 Author chain C; PDBConstruct 1–452; UniProt 1–452 Author chain D; PDBConstruct 1–452; UniProt 1–452 Author chain E; PDBConstruct 1–452; UniProt 1–452 |