Research workbench
Human mabs broadly protect against infection of arthritiogenic alphaviruses by recognizing conserved elements of the MXR8 receptor binding domain
Analyse Human mabs broadly protect against infection of arthritiogenic alphaviruses by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VYV
- Type
- protein
- Length
- 4,652 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E1 glycoprotein; E2 glycoprotein; Fab chk-265 heavy chain; Fab chk-265 light chain
- EC
- 3.4.21.90
- UniProt
- P08491
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · 4 distinct chains · 3% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | E1 glycoprotein (EC 3.4.21.90) | protein | 393 | 3% helix, 30% strand | P08491 |
| E, F, G, H | E2 glycoprotein (EC 3.4.21.90) | protein | 341 | 2% helix, 31% strand | P08491 |
| I, J, K, L | Fab chk-265 heavy chain | protein | 218 | 4% helix, 42% strand | — |
| M, N, O, P | Fab chk-265 light chain | protein | 211 | 4% helix, 42% strand | — |
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 | 865 | 0.77 | 0.81 | 110 | empty |
| 2 | 708 | 0.76 | 0.82 | 89 | empty |
| 3 | 471 | 0.75 | 0.85 | 87 | empty |
| 4 | 1038 | 0.74 | 0.78 | 156 | empty |
| 5 | 1024 | 0.74 | 0.78 | 125 | empty |
Interfaces
22 interfaces between chains.
- B–F · 697 Ų buried · 10 hydrogen bonds · protein-protein
- A–E · 656 Ų buried · 9 hydrogen bonds · protein-protein
- C–G · 630 Ų buried · 12 hydrogen bonds · protein-protein
- D–H · 582 Ų buried · 9 hydrogen bonds · protein-protein
- J–N · 347 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6VYV · Human mAbs broadly protect against infection of arthritiogenic alphaviruses by… · 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 P08491
- Elsewhere: RCSB PDB 6VYV · PDBe 6VYV · UniProt P08491
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