Research workbench
Fit of E protein and Fab 1A1D-2 into 24 ångström resolution cryoem MAP of Fab complexed with dengue 2 virus.
Analyse Fit of E protein and Fab 1A1D-2 into 24 ångström resolution cryoem MAP of Fab… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R6P
- Type
- protein
- Length
- 2,006 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major envelope protein E; Heavy chain of 1A1D-2; Light chain of 1A1D-2
- UniProt
- P18356
- Pockets
- 3 · best druggability 0.43
Structure
electron microscopy · 4 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Major envelope protein E | protein | 386 | 0% helix, 0% strand | P18356 |
| B | Major envelope protein E | protein | 390 | 0% helix, 0% strand | P18356 |
| D, F | Heavy chain of 1A1D-2 | protein | 216 | 0% helix, 0% strand | — |
| E, G | Light chain of 1A1D-2 | protein | 206 | 0% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.43 | 0.73 | 40 | empty |
| 2 | 74 | 0.33 | 0.73 | 23 | empty |
| 3 | 73 | 0.33 | 0.73 | 25 | empty |
Interfaces
6 interfaces between chains.
- F–G · 133 Ų buried · 0 hydrogen bonds · protein-protein
- D–E · 132 Ų buried · 0 hydrogen bonds · protein-protein
- C–F · 38 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 38 Ų buried · 0 hydrogen bonds · protein-protein
- A–E · 37 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2R6P · Fit of E protein and Fab 1A1D-2 into 24 angstrom resolution cryoEM map of Fab complexed… · 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 P18356
- Elsewhere: RCSB PDB 2R6P · PDBe 2R6P · UniProt P18356
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