Research workbench
Crystal Structure of Novel Immune-Type Receptor 11 Extracellular Fragment Mutant N30D
Analyse Crystal Structure of Novel Immune-Type Receptor 11 Extracellular Fragment… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QTE
- Type
- protein
- Length
- 436 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Ictalurus punctatus
- Molecule
- Novel immune-type receptor 11
- UniProt
- Q8UWK4
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 6% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Novel immune-type receptor 11 | protein | 109 | 6% helix, 51% strand | Q8UWK4 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 614 | 0.78 | 0.84 | 69 | empty |
| 2 | 82 | 0.37 | 0.76 | 19 | empty |
| 3 | 50 | 0.36 | 0.80 | 13 | empty |
| 4 | 84 | 0.34 | 0.75 | 20 | empty |
| 5 | 52 | 0.29 | 0.76 | 14 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1329 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1304 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 360 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 344 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 291 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2QTE · Crystal structure of novel immune-type receptor 11 extracellular fragment mutant N30D · 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 Q8UWK4
- Elsewhere: RCSB PDB 2QTE · PDBe 2QTE · UniProt Q8UWK4
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