Research workbench
Crystal structure of ev-D68-3DPOL in complex with GTP
Analyse Crystal structure of ev-D68-3DPOL in complex with GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XE0
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Genome polyprotein
- UniProt
- F1T146
- Ligands
- GTP
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Genome polyprotein | protein | 457 | 43% helix, 16% strand | F1T146 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.64 | 0.78 | 46 | GTP |
| 2 | 219 | 0.55 | 0.78 | 30 | empty |
| 3 | 117 | 0.44 | 0.77 | 18 | empty |
Compared structures
- 5XE0 · Crystal structure of EV-D68-3Dpol in complex with GTP · 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 F1T146
- Elsewhere: RCSB PDB 5XE0 · PDBe 5XE0 · UniProt F1T146
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