Research workbench
Structure of wind Y53F mutant
Analyse Structure of wind Y53F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C0F
- Type
- protein
- Length
- 451 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Windbeutel protein
- UniProt
- O44342
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Windbeutel protein | protein | 228 | 49% helix, 11% strand | O44342 |
| B | Windbeutel protein | protein | 223 | 52% helix, 12% strand | O44342 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 343 | 0.54 | 0.74 | 44 | empty |
| 2 | 220 | 0.51 | 0.76 | 44 | empty |
| 3 | 81 | 0.36 | 0.76 | 17 | empty |
| 4 | 103 | 0.34 | 0.73 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 904 Ų buried · 8 hydrogen bonds · protein-protein
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 O44342
- Elsewhere: RCSB PDB 2C0F · PDBe 2C0F · UniProt O44342
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