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Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK2 (KIR3.2) in apo form
Analyse Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XIS
- Type
- protein
- Length
- 1,240 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- G protein-activated inward rectifier potassium channel 2
- UniProt
- A0A338P6L0
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 1 distinct chain · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | G protein-activated inward rectifier potassium channel 2 | protein | 310 | 29% helix, 23% strand | A0A338P6L0 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1024 | 0.87 | 0.87 | 108 | empty |
| 2 | 978 | 0.75 | 0.78 | 72 | empty |
| 3 | 517 | 0.74 | 0.82 | 68 | empty |
| 4 | 509 | 0.72 | 0.81 | 62 | empty |
| 5 | 358 | 0.70 | 0.83 | 46 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2098 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 2071 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 2053 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 2040 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 25 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6XIS · Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK2 (Kir3.2) in… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A338P6L0
- Elsewhere: RCSB PDB 6XIS · PDBe 6XIS · UniProt A0A338P6L0
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