Research workbench
Structure of deinococcus radiodurans tunicamycin resistance protein
Analyse Structure of deinococcus radiodurans tunicamycin resistance protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VLI
- Type
- protein
- Length
- 337 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antibiotic resistance protein
- UniProt
- Q9RUG7
- Ligands
- CD, CL
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antibiotic resistance protein | protein | 164 | 51% helix, 13% strand | Q9RUG7 |
| B | Antibiotic resistance protein | protein | 173 | 53% helix, 13% strand | Q9RUG7 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 559 | 0.66 | 0.77 | 61 | empty |
| 2 | 88 | 0.45 | 0.80 | 16 | empty |
| 3 | 60 | 0.39 | 0.80 | 17 | empty |
| 4 | 80 | 0.36 | 0.76 | 19 | empty |
| 5 | 57 | 0.36 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 499 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2VLI · Structure of Deinococcus radiodurans tunicamycin resistance protein · 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 Q9RUG7
- Elsewhere: RCSB PDB 2VLI · PDBe 2VLI · UniProt Q9RUG7
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