Research workbench
Cryo-EM structure of the human concentrative nucleoside transporter CNT3
Analyse Cryo-EM structure of the human concentrative nucleoside transporter CNT3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KSW
- Type
- protein
- Length
- 1,539 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.6
- Source
- Homo sapiens
- Molecule
- Solute carrier family 28 member 3
- UniProt
- Q9HAS3
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · resolution 3.6 · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, A, B | Solute carrier family 28 member 3 | protein | 513 | 73% helix, 0% strand | Q9HAS3 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.88 | 0.92 | 42 | empty |
| 2 | 847 | 0.72 | 0.76 | 59 | empty |
| 3 | 889 | 0.72 | 0.76 | 57 | empty |
| 4 | 435 | 0.72 | 0.82 | 46 | empty |
| 5 | 801 | 0.71 | 0.76 | 61 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1670 Ų buried · 10 hydrogen bonds · protein-protein
- C–B · 1665 Ų buried · 10 hydrogen bonds · protein-protein
- C–A · 1662 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6KSW · Cryo-EM structure of the human concentrative nucleoside transporter CNT3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HAS3 · AlphaFold monomer V2.0 prediction for solute carrier family 28 member 3 (Q9HAS3) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 Q9HAS3
- Elsewhere: RCSB PDB 6KSW · PDBe 6KSW · UniProt Q9HAS3
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