MolNFT v2 · #5858 · protein
ECHOVIRUS 1
1EV1: “ECHOVIRUS 1”. X-ray diffraction at 3.55, 2 ligands (PLM, MYR), 11 pockets (best druggability 0.76). MolNFT v2 #5858 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1EV1
- Type
- protein
- Length
- 835 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.55
- Source
- Human echovirus 1
- Molecule
- Echovirus 1
- UniProt
- O91734
- Ligands
- PLM, MYR
- Pockets
- 11 · best druggability 0.76
Structure
x-ray diffraction · resolution 3.55 · 4 distinct chains · 12% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Echovirus 1 | protein | 281 | 11% helix, 33% strand | O91734 |
| 2 | Echovirus 1 | protein | 254 | 13% helix, 37% strand | O91734 |
| 3 | Echovirus 1 | protein | 239 | 13% helix, 32% strand | O91734 |
| 4 | Echovirus 1 | protein | 61 | 11% helix, 16% strand | O91734 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.76 | 0.84 | 74 | PLM |
| 2 | 423 | 0.58 | 0.74 | 57 | empty |
| 3 | 80 | 0.56 | 0.87 | 16 | empty |
| 4 | 75 | 0.50 | 0.84 | 16 | empty |
| 5 | 121 | 0.47 | 0.78 | 20 | empty |
Interfaces
6 interfaces between chains.
- 1–3 · 4324 Ų buried · 82 hydrogen bonds · protein-protein
- 1–2 · 2088 Ų buried · 36 hydrogen bonds · protein-protein
- 2–3 · 1678 Ų buried · 24 hydrogen bonds · protein-protein
- 1–4 · 1618 Ų buried · 19 hydrogen bonds · protein-protein
- 3–4 · 952 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 1EV1 · ECHOVIRUS 1 · the same entry in another collection · chain 1 against 1, 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 O91734
- Elsewhere: RCSB PDB 1EV1 · PDBe 1EV1 · UniProt O91734
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