Research workbench
Foot-and-mouth disease virus/ oligosaccharide receptor complex.
Analyse Foot-and-mouth disease virus/ oligosaccharide receptor complex. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QQP
- Type
- protein
- Length
- 670 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (genome polyprotein)
- UniProt
- P03305
- Ligands
- IDX, SGN, IDS
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 12% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Protein (genome polyprotein) | protein | 188 | 14% helix, 29% strand | P03305 |
| 2 | Protein (genome polyprotein) | protein | 216 | 12% helix, 43% strand | P03305 |
| 3 | Protein (genome polyprotein) | protein | 220 | 9% helix, 33% strand | P03305 |
| 4 | Protein (genome polyprotein) | protein | 46 | 24% helix, 2% strand | P03305 |
Ligands and binding sites
- IDX · 2-O-sulfo-alpha-L-gulopyranuronic acid · ligand · 2 copies · chains 1
- SGN · 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose · sugar · 2 copies · chains 1, 2
- IDS · 2-O-sulfo-alpha-L-idopyranuronic acid · sugar · chains 1, 2
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 981 | 0.78 | 0.79 | 90 | empty |
| 2 | 456 | 0.70 | 0.81 | 49 | empty |
| 3 | 210 | 0.53 | 0.77 | 29 | empty |
| 4 | 96 | 0.45 | 0.79 | 17 | empty |
| 5 | 150 | 0.43 | 0.75 | 24 | empty |
Interfaces
6 interfaces between chains.
- 1–2 · 1391 Ų buried · 17 hydrogen bonds · protein-protein
- 1–3 · 1047 Ų buried · 18 hydrogen bonds · protein-protein
- 2–3 · 930 Ų buried · 10 hydrogen bonds · protein-protein
- 1–4 · 785 Ų buried · 17 hydrogen bonds · protein-protein
- 2–4 · 329 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1QQP · Foot-and-mouth disease virus/ oligosaccharide receptor complex. · 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 P03305
- Elsewhere: RCSB PDB 1QQP · PDBe 1QQP · UniProt P03305
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