MolNFT v1 · #184578 · protein
Wilavidin apo form (P1 form)
7OUR: “Wilavidin apo form (P1 form)”. X-ray diffraction, 7 pockets (best druggability 0.75). MolNFT v1 #184578 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7OUR
- Type
- protein
- Length
- 713 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wilavidin
- UniProt
- A0A3A4VWA2
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 5 distinct chains · 3% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Wilavidin | protein | 118 | 3% helix, 62% strand | A0A3A4VWA2 |
| C | Wilavidin | protein | 119 | 3% helix, 63% strand | A0A3A4VWA2 |
| F | Wilavidin | protein | 121 | 2% helix, 60% strand | A0A3A4VWA2 |
| B | Wilavidin | protein | 120 | 3% helix, 59% strand | A0A3A4VWA2 |
| E | Wilavidin | protein | 117 | 3% helix, 63% strand | A0A3A4VWA2 |
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 798 | 0.75 | 0.80 | 84 | empty |
| 2 | 60 | 0.60 | 0.91 | 15 | empty |
| 3 | 52 | 0.58 | 0.91 | 15 | empty |
| 4 | 54 | 0.58 | 0.91 | 15 | empty |
| 5 | 55 | 0.58 | 0.90 | 15 | empty |
Interfaces
12 interfaces between chains.
- A–B · 1751 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1741 Ų buried · 16 hydrogen bonds · protein-protein
- F–E · 1730 Ų buried · 16 hydrogen bonds · protein-protein
- D–E · 1639 Ų buried · 19 hydrogen bonds · protein-protein
- A–F · 1632 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 7OUR · Wilavidin apo form (P1 form) · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A3A4VWA2
- Elsewhere: RCSB PDB 7OUR · PDBe 7OUR · UniProt A0A3A4VWA2
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