MolNFT v1 · #187225 · protein
Human katp channel in open conformation, focused on sur
7S5V · ATP-binding cassette sub-family C member 8: “Human katp channel in open conformation, focused on sur”. Electron microscopy, 3 ligands (ADP, ATP, MG), 15 pockets (best druggability 0.84). MolNFT v1 #187225 on GenesisL1: 3D structure…
- PDB
- 7S5V
- Type
- protein
- Length
- 1,397 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-binding cassette sub-family C member 8
- UniProt
- Q09428
- Ligands
- ADP, ATP, MG
- Pockets
- 15 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 56% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | ATP-binding cassette sub-family C member 8 | protein | 1397 | 56% helix, 7% strand | Q09428 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains E
- ATP · Adenosine-5'-triphosphate · ligand · chains E
- MG · Magnesium ion · metal · 2 copies · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 558 | 0.84 | 0.90 | 75 | MG, ATP |
| 2 | 520 | 0.83 | 0.90 | 58 | empty |
| 3 | 158 | 0.81 | 0.96 | 23 | empty |
| 4 | 87 | 0.74 | 0.97 | 23 | empty |
| 5 | 641 | 0.66 | 0.75 | 71 | empty |
Compared structures
- 7S5V · Human KATP channel in open conformation, focused on SUR · the same entry in another collection · chain E against E, TM-score 1.00
- 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 0.87
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 Q09428
- Elsewhere: RCSB PDB 7S5V · PDBe 7S5V · UniProt Q09428
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