Research workbench
Trypanosoma brucei ISG65 bound to human complement C3D
Analyse Trypanosoma brucei ISG65 bound to human complement C3D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PI6
- Type
- protein
- Length
- 996 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 65 kda invariant surface glycoprotein; Complement C3DG fragment
- UniProt
- Q587F5, P01024
- Pockets
- 12 · best druggability 0.63
Structure
x-ray diffraction · 4 distinct chains · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 65 kda invariant surface glycoprotein | protein | 221 | 79% helix, 1% strand | Q587F5 |
| B | Complement C3DG fragment | protein | 290 | 61% helix, 2% strand | P01024 |
| C | 65 kda invariant surface glycoprotein | protein | 196 | 87% helix, 0% strand | Q587F5 |
| D | Complement C3DG fragment | protein | 289 | 60% helix, 2% strand | P01024 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains A, B, C, D
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 385 | 0.63 | 0.78 | 43 | GOL |
| 2 | 335 | 0.57 | 0.76 | 31 | empty |
| 3 | 326 | 0.55 | 0.75 | 28 | empty |
| 4 | 163 | 0.48 | 0.77 | 22 | empty |
| 5 | 177 | 0.46 | 0.75 | 21 | empty |
Interfaces
3 interfaces between chains.
- C–D · 883 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 858 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 597 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 Q587F5
- Every structure of UniProt P01024
- Elsewhere: RCSB PDB 7PI6 · PDBe 7PI6 · UniProt Q587F5 · UniProt P01024
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.