Research workbench
Complex structure of mab 4.2-scfv with tick-borne encephalitis virus envelope protein
Analyse Complex structure of mab 4.2-scfv with tick-borne encephalitis virus envelope… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J5G
- Type
- protein
- Length
- 601 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope protein E; Antibody heavy chain; Antibody light chain
- UniProt
- P14336
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 7% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Envelope protein E | protein | 373 | 8% helix, 49% strand | P14336 |
| H | Antibody heavy chain | protein | 120 | 8% helix, 52% strand | — |
| L | Antibody light chain | protein | 108 | 3% helix, 47% strand | — |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 280 | 0.75 | 0.87 | 38 | empty |
| 2 | 109 | 0.61 | 0.87 | 27 | empty |
| 3 | 381 | 0.60 | 0.76 | 37 | empty |
| 4 | 159 | 0.44 | 0.75 | 36 | empty |
| 5 | 65 | 0.43 | 0.81 | 18 | empty |
Interfaces
3 interfaces between chains.
- H–L · 788 Ų buried · 8 hydrogen bonds · protein-protein
- A–H · 383 Ų buried · 10 hydrogen bonds · protein-protein
- A–L · 344 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6J5G · Complex structure of MAb 4.2-scFv with tick-borne encephalitis virus envelope protein · 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 P14336
- Elsewhere: RCSB PDB 6J5G · PDBe 6J5G · UniProt P14336
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