Research workbench
A complex of two editosome proteins and two nanobodies
Analyse A complex of two editosome proteins and two nanobodies in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3STB
- Type
- protein
- Length
- 470 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Single domain antibody vhh; RNA-editing complex protein MP42; MP18 RNA editing complex…
- UniProt
- Q95W13, Q38B90
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 4 distinct chains · 10% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Single domain antibody vhh | protein | 125 | 10% helix, 50% strand | — |
| B | Single domain antibody vhh | protein | 126 | 10% helix, 53% strand | — |
| C | RNA-editing complex protein MP42 | protein | 111 | 9% helix, 60% strand | Q95W13 |
| D | MP18 RNA editing complex protein | protein | 108 | 12% helix, 53% strand | Q38B90 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.64 | 0.81 | 51 | empty |
| 2 | 298 | 0.61 | 0.79 | 39 | empty |
| 3 | 189 | 0.54 | 0.79 | 33 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1661 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 964 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 895 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 429 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 351 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3STB · A complex of two editosome proteins and two nanobodies · 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 Q95W13
- Every structure of UniProt Q38B90
- Elsewhere: RCSB PDB 3STB · PDBe 3STB · UniProt Q95W13 · UniProt Q38B90
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