Research workbench
X-ray crystal structure of truncated human chemokine CCL19 (7-70)
Analyse X-ray crystal structure of truncated human chemokine CCL19 (7-70) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7STA
- Type
- protein
- Length
- 250 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-C motif chemokine 19
- UniProt
- Q99731
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | C-C motif chemokine 19 | protein | 64 | 28% helix, 28% strand | Q99731 |
| B, D | C-C motif chemokine 19 | protein | 61 | 30% helix, 30% strand | Q99731 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.36 | 0.74 | 22 | empty |
Interfaces
3 interfaces between chains.
- C–D · 703 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 689 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 39 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 Q99731
- Elsewhere: RCSB PDB 7STA · PDBe 7STA · UniProt Q99731
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