Research workbench
F80A mutant of the urea transporter from desulfovibrio vulgaris
Analyse F80A mutant of the urea transporter from desulfovibrio vulgaris in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M6E
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative urea transporter
- UniProt
- Q72CX3
- Ligands
- AU
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative urea transporter | protein | 333 | 70% helix, 1% strand | Q72CX3 |
Ligands and binding sites
- AU · Gold ion · metal · 9 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 | 332 | 0.61 | 0.78 | 33 | empty |
| 2 | 237 | 0.60 | 0.80 | 31 | AU |
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 Q72CX3
- Elsewhere: RCSB PDB 3M6E · PDBe 3M6E · UniProt Q72CX3
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