Research workbench
KIRBAC3.1 C71S C262S
Analyse KIRBAC3.1 C71S C262S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N9L
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inward rectifier potassium channel KIRBAC3.1
- UniProt
- D9N164
- Ligands
- PCW, TMO, K
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inward rectifier potassium channel KIRBAC3.1 | protein | 282 | 31% helix, 32% strand | D9N164 |
Ligands and binding sites
- PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · 4 copies · chains A
- TMO · trimethylamine oxide · ligand · chains A
- K · Potassium ion · metal · 9 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.32 | 0.73 | 13 | PCW |
Compared structures
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 D9N164
- Elsewhere: RCSB PDB 7N9L · PDBe 7N9L · UniProt D9N164
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