Research workbench
Human katp channel in open conformation, focused on kir and one sur, position 3
Analyse Human katp channel in open conformation, focused on kir and one sur, position 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S5Z
- Type
- protein
- Length
- 2,687 residues
- Chains
- 5
- 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
- B2RC52, Q09428
- Ligands
- ADP, ATP, MG
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 2 distinct chains · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | ATP-sensitive inward rectifier potassium channel 11 | protein | 321 | 31% helix, 27% strand | B2RC52 |
| E | ATP-binding cassette sub-family C member 8 | protein | 1403 | 60% helix, 8% 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
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 | 1065 | 0.89 | 0.90 | 86 | empty |
| 2 | 652 | 0.86 | 0.91 | 90 | empty |
| 3 | 441 | 0.83 | 0.90 | 72 | MG, ATP |
| 4 | 183 | 0.82 | 0.96 | 33 | empty |
| 5 | 86 | 0.72 | 0.96 | 21 | empty |
Interfaces
8 interfaces between chains.
- C–D · 3429 Ų buried · 40 hydrogen bonds · protein-protein
- A–D · 3413 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 3409 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 3404 Ų buried · 39 hydrogen bonds · protein-protein
- B–E · 1457 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7S5Z · Human KATP channel in open conformation, focused on Kir and one SUR, position 3 · the same entry in another collection · chain A against A, 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 0.86
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 B2RC52
- Every structure of UniProt Q09428
- Elsewhere: RCSB PDB 7S5Z · PDBe 7S5Z · UniProt B2RC52 · UniProt Q09428
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