Research workbench
Cryo-EM structure of human katp bound to ATP and ADP in quatrefoil form
Analyse Cryo-EM structure of human katp bound to ATP and ADP in quatrefoil form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C3O
- Type
- protein
- Length
- 6,472 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-sensitive inward rectifier potassium channel 11; ATP-binding cassette sub-family C…
- UniProt
- Q14654, Q09428
- Ligands
- ATP, ADP, MG, K
- Pockets
- 20 · best druggability 0.90
Structure
electron microscopy · 2 distinct chains · 57% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B, D | ATP-sensitive inward rectifier potassium channel 11 | protein | 328 | 29% helix, 28% strand | Q14654 |
| E, H, G, F | ATP-binding cassette sub-family C member 8 | protein | 1290 | 65% helix, 8% strand | Q09428 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 8 copies · chains A, B, C, D, E, H, G, F
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains E, H, G, F
- MG · Magnesium ion · metal · 8 copies · chains E, H, G, F
- K · Potassium ion · metal · 3 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1022 | 0.90 | 0.92 | 129 | empty |
| 2 | 1000 | 0.90 | 0.92 | 132 | empty |
| 3 | 919 | 0.89 | 0.92 | 120 | empty |
| 4 | 713 | 0.88 | 0.92 | 107 | empty |
| 5 | 909 | 0.86 | 0.88 | 86 | empty |
Interfaces
14 interfaces between chains.
- C–D · 3110 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 3106 Ų buried · 34 hydrogen bonds · protein-protein
- C–B · 3092 Ų buried · 33 hydrogen bonds · protein-protein
- A–D · 3083 Ų buried · 33 hydrogen bonds · protein-protein
- C–G · 1275 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6C3O · Cryo-EM structure of human KATP bound to ATP and ADP in quatrefoil form · the same entry in another collection · chain F against F, TM-score 1.00
- Q14654 · AlphaFold monomer V2.0 prediction for ATP-sensitive inward rectifier potassium channel 11… · a predicted model of the same protein · chain A against A, TM-score 0.95
- Q09428 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family C member 8 (Q09428) · a predicted model of the same protein · chain E against A, TM-score 0.75
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 Q14654
- Every structure of UniProt Q09428
- Elsewhere: RCSB PDB 6C3O · PDBe 6C3O · UniProt Q14654 · UniProt Q09428
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