MolNFT v1 · #141106 · protein
Structure of pancreatic ATP-sensitive potassium channel bound with mg- ADP (focused refinement of SUR1 ABC transporter module at 4.22A)
5YWD · ATP-binding cassette sub-family C member 8 isoform X2: “Structure of pancreatic ATP-sensitive potassium channel bound with mg- ADP (focused refinement of SUR1 ABC…”. Electron microscopy, 2 ligands (ADP, MG), 20 pockets (best…
- PDB
- 5YWD
- Type
- protein
- Length
- 1,154 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-binding cassette sub-family C member 8 isoform X2
- UniProt
- A0A1U7R319
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 64% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | ATP-binding cassette sub-family C member 8 isoform X2 | protein | 1154 | 64% helix, 8% strand | A0A1U7R319 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains B
- MG · Magnesium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 305 | 0.84 | 0.94 | 46 | empty |
| 2 | 198 | 0.80 | 0.94 | 30 | empty |
| 3 | 221 | 0.78 | 0.93 | 39 | empty |
| 4 | 214 | 0.78 | 0.92 | 38 | empty |
| 5 | 188 | 0.77 | 0.92 | 35 | empty |
Compared structures
- 5YWD · Structure of pancreatic ATP-sensitive potassium channel bound with Mg-ADP (focused… · the same entry in another collection · chain B against B, 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 A0A1U7R319
- Elsewhere: RCSB PDB 5YWD · PDBe 5YWD · UniProt A0A1U7R319
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