MolNFT v1 · #63333 · protein
Crystal structure of the virion-associated protein P3 from caulimovirus
3F6N: “Crystal structure of the virion-associated protein P3 from caulimovirus”. X-ray diffraction, 3 pockets (best druggability 0.83). MolNFT v1 #63333 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3F6N
- Type
- protein
- Length
- 289 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Virion-associated protein
- UniProt
- P03551
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Virion-associated protein | protein | 70 | 86% helix, 0% strand | P03551 |
| B | Virion-associated protein | protein | 74 | 82% helix, 0% strand | P03551 |
| C | Virion-associated protein | protein | 73 | 79% helix, 0% strand | P03551 |
| D | Virion-associated protein | protein | 72 | 81% helix, 0% strand | P03551 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.83 | 0.97 | 27 | empty |
| 2 | 69 | 0.75 | 0.98 | 18 | empty |
| 3 | 200 | 0.60 | 0.81 | 33 | empty |
Interfaces
6 interfaces between chains.
- A–C · 1720 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 1671 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1639 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 1609 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 256 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3F6N · Crystal structure of the virion-associated protein P3 from Caulimovirus · the same entry in another collection · chain D against D, 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 P03551
- Elsewhere: RCSB PDB 3F6N · PDBe 3F6N · UniProt P03551
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