Research workbench
Cryo-EM structure of the pancreatic beta-cell SUR1 bound to ATP only
Analyse Cryo-EM structure of the pancreatic beta-cell SUR1 bound to ATP only in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PZI
- Type
- protein
- Length
- 1,412 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-binding cassette sub-family C member 8
- UniProt
- Q09427
- Ligands
- ATP
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 62% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G | ATP-binding cassette sub-family C member 8 | protein | 1412 | 62% helix, 6% strand | Q09427 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.84 | 0.85 | 100 | empty |
| 2 | 457 | 0.80 | 0.88 | 70 | empty |
| 3 | 544 | 0.80 | 0.86 | 102 | empty |
| 4 | 455 | 0.79 | 0.87 | 67 | empty |
| 5 | 535 | 0.79 | 0.86 | 73 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6PZI · Cryo-EM structure of the pancreatic beta-cell SUR1 bound to ATP only · the same entry in another collection · chain G against G, TM-score 1.00
- Q09427 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family C member 8 (Q09427) · a predicted model of the same protein · chain G against A, TM-score 0.98
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 Q09427
- Elsewhere: RCSB PDB 6PZI · PDBe 6PZI · UniProt Q09427
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