Research workbench
Cryoem structure of mayaro virus icosahedral subunit
Analyse Cryoem structure of mayaro virus icosahedral subunit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LIH
- Type
- protein
- Length
- 4,008 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein; E1 protein; E2 protein
- UniProt
- Q8QZ72, A0A0P0CE34, A0A0P0BWJ4
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 3 distinct chains · 9% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, A, B, C | Capsid protein | protein | 160 | 6% helix, 43% strand | Q8QZ72 |
| T, H, I, J | E1 protein | protein | 435 | 8% helix, 29% strand | A0A0P0CE34 |
| M, D, E, G | E2 protein | protein | 407 | 12% helix, 28% strand | A0A0P0BWJ4 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 968 | 0.82 | 0.84 | 93 | empty |
| 2 | 745 | 0.80 | 0.83 | 93 | empty |
| 3 | 552 | 0.78 | 0.85 | 61 | empty |
| 4 | 398 | 0.78 | 0.87 | 60 | empty |
| 5 | 652 | 0.76 | 0.82 | 75 | empty |
Interfaces
25 interfaces between chains.
- T–M · 2937 Ų buried · 11 hydrogen bonds · protein-protein
- I–E · 2936 Ų buried · 11 hydrogen bonds · protein-protein
- J–G · 2931 Ų buried · 11 hydrogen bonds · protein-protein
- H–D · 2929 Ų buried · 11 hydrogen bonds · protein-protein
- M–D · 593 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 52 disulfide (disulfide).
Compared structures
- 7LIH · CryoEM structure of Mayaro virus icosahedral subunit · the same entry in another collection · chain F against F, 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 Q8QZ72
- Every structure of UniProt A0A0P0CE34
- Every structure of UniProt A0A0P0BWJ4
- Elsewhere: RCSB PDB 7LIH · PDBe 7LIH · UniProt Q8QZ72 · UniProt A0A0P0CE34 · UniProt A0A0P0BWJ4
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