Research workbench
Chloride intracellular channel 1 (CLIC1) complexed with glutathione
Analyse Chloride intracellular channel 1 (CLIC1) complexed with glutathione in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K0N
- Type
- protein
- Length
- 445 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chloride intracellular channel protein 1
- UniProt
- O00299
- Ligands
- GSH
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chloride intracellular channel protein 1 | protein | 226 | 49% helix, 9% strand | O00299 |
| B | Chloride intracellular channel protein 1 | protein | 219 | 50% helix, 11% strand | O00299 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.56 | 0.75 | 33 | empty |
| 2 | 66 | 0.29 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 154 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1K0N · Chloride Intracellular Channel 1 (CLIC1) complexed with glutathione · the same entry in another collection · chain A against A, TM-score 1.00
- O00299 · AlphaFold monomer V2.0 prediction for chloride intracellular channel protein 1 (O00299) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 O00299
- Elsewhere: RCSB PDB 1K0N · PDBe 1K0N · UniProt O00299
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