Research workbench
Short form D7 protein from culex quinquefasciatus
Analyse Short form D7 protein from culex quinquefasciatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TVY
- Type
- protein
- Length
- 549 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Salivary short D7 protein 3
- UniProt
- Q6TS00
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.48
Structure
x-ray diffraction · 3 distinct chains · 50% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Salivary short D7 protein 3 | protein | 138 | 49% helix, 1% strand | Q6TS00 |
| B | Salivary short D7 protein 3 | protein | 139 | 50% helix, 1% strand | Q6TS00 |
| D | Salivary short D7 protein 3 | protein | 134 | 51% helix, 1% strand | Q6TS00 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.48 | 0.79 | 23 | empty |
| 2 | 116 | 0.36 | 0.73 | 18 | empty |
| 3 | 63 | 0.33 | 0.76 | 17 | empty |
| 4 | 67 | 0.32 | 0.75 | 16 | empty |
Interfaces
4 interfaces between chains.
- A–B · 425 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 118 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 89 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 19 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 7TVY · Short form D7 protein from Culex quinquefasciatus · 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 Q6TS00
- Elsewhere: RCSB PDB 7TVY · PDBe 7TVY · UniProt Q6TS00
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