Research workbench
Crystal structure of the tick evasin eva-P974 complexed to human chemokine CCL17
Analyse Crystal structure of the tick evasin eva-P974 complexed to human chemokine CCL17 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S4N
- Type
- protein
- Length
- 296 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Evasin P974; C-C motif chemokine 17
- UniProt
- A0A023FDY8, Q92583
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 4 distinct chains · 14% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Evasin P974 | protein | 82 | 5% helix, 51% strand | A0A023FDY8 |
| C | Evasin P974 | protein | 84 | 7% helix, 49% strand | A0A023FDY8 |
| D | C-C motif chemokine 17 | protein | 67 | 22% helix, 25% strand | Q92583 |
| B | C-C motif chemokine 17 | protein | 63 | 25% helix, 27% strand | Q92583 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 357 | 0.52 | 0.73 | 40 | empty |
| 2 | 60 | 0.36 | 0.78 | 16 | empty |
Interfaces
4 interfaces between chains.
- C–D · 916 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 798 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 46 Ų buried · 0 hydrogen bonds · protein-protein
- D–B · 36 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 7S4N · Crystal structure of the tick evasin EVA-P974 complexed to human chemokine CCL17 · the same entry in another collection · chain A against A, TM-score 1.00
- Q92583 · AlphaFold monomer V2.0 prediction for C-C motif chemokine 17 (Q92583) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 A0A023FDY8
- Every structure of UniProt Q92583
- Elsewhere: RCSB PDB 7S4N · PDBe 7S4N · UniProt A0A023FDY8 · UniProt Q92583
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