Research workbench
X-ray structure of the human urea channel SLC14A1/UT1
Analyse X-ray structure of the human urea channel SLC14A1/UT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QD5
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Urea transporter 1
- UniProt
- Q13336
- Ligands
- Y01
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Urea transporter 1 | protein | 356 | 71% helix, 1% strand | Q13336 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · chains A
- BOG · octyl beta-D-glucopyranoside · additive · 7 copies · chains A
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 417 | 0.67 | 0.79 | 44 | PG4 |
| 2 | 343 | 0.67 | 0.81 | 42 | BOG |
Compared structures
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 Q13336
- Elsewhere: RCSB PDB 6QD5 · PDBe 6QD5 · UniProt Q13336
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