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Crystal structure of chicken bok
Analyse Crystal structure of chicken bok in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WDD
- Type
- protein
- Length
- 309 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-related ovarian killer protein
- UniProt
- Q9I8I2
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BCL-2-related ovarian killer protein | protein | 150 | 77% helix, 0% strand | Q9I8I2 |
| B | BCL-2-related ovarian killer protein | protein | 159 | 72% helix, 0% strand | Q9I8I2 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 510 | 0.64 | 0.76 | 39 | EDO |
| 2 | 329 | 0.61 | 0.78 | 37 | EDO |
| 3 | 122 | 0.57 | 0.84 | 20 | empty |
| 4 | 84 | 0.32 | 0.73 | 18 | EDO |
Interfaces
1 interface between chains.
- A–B · 622 Ų buried · 10 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 Q9I8I2
- Elsewhere: RCSB PDB 5WDD · PDBe 5WDD · UniProt Q9I8I2
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