Research workbench
Crystal structure of bacteriorhodopsin mutant T46A
Analyse Crystal structure of bacteriorhodopsin mutant T46A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UTX
- Type
- protein
- Length
- 454 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacteriorhodopsin
- UniProt
- P02945
- Ligands
- RET, D12
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bacteriorhodopsin | protein | 227 | 78% helix, 5% strand | P02945 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.81 | 0.97 | 23 | RET |
| 2 | 118 | 0.79 | 0.98 | 21 | RET |
| 3 | 222 | 0.69 | 0.85 | 31 | empty |
| 4 | 97 | 0.56 | 0.84 | 18 | empty |
| 5 | 188 | 0.46 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 787 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (retinal Schiff base).
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 P02945
- Elsewhere: RCSB PDB 3UTX · PDBe 3UTX · UniProt P02945
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