Research workbench
Killer toxin from halotolerant yeast
Analyse Killer toxin from halotolerant yeast in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KVE
- Type
- protein
- Length
- 280 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Smk toxin
- UniProt
- P19972
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Smk toxin | protein | 63 | 41% helix, 25% strand | P19972 |
| B, D | Smk toxin | protein | 77 | 21% helix, 36% strand | P19972 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 537 | 0.68 | 0.78 | 69 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2423 Ų buried · 50 hydrogen bonds · protein-protein
- A–B · 2416 Ų buried · 45 hydrogen bonds · protein-protein
- A–C · 432 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 155 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 31 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 P19972
- Elsewhere: RCSB PDB 1KVE · PDBe 1KVE · UniProt P19972
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