Research workbench
Crystal structure of tetracycline destructase TET(50) in complex with anhydrotetracycline
Analyse Crystal structure of tetracycline destructase TET(50) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TUF
- Type
- protein
- Length
- 759 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetracycline destructase TET(50)
- UniProt
- A0A059WYP6
- Ligands
- FAD, TDC, SO4
- Pockets
- 5 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetracycline destructase TET(50) | protein | 388 | 36% helix, 26% strand | A0A059WYP6 |
| B | Tetracycline destructase TET(50) | protein | 371 | 34% helix, 29% strand | A0A059WYP6 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- TDC · 5A,6-anhydrotetracycline · ligand · chains B
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.84 | 0.89 | 71 | FAD, TDC |
| 2 | 519 | 0.84 | 0.90 | 75 | SO4, FAD |
| 3 | 111 | 0.65 | 0.89 | 24 | empty |
| 4 | 166 | 0.57 | 0.82 | 28 | empty |
| 5 | 120 | 0.53 | 0.82 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 829 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5TUF · Crystal structure of tetracycline destructase Tet(50) in complex with anhydrotetracycline · 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 A0A059WYP6
- Elsewhere: RCSB PDB 5TUF · PDBe 5TUF · UniProt A0A059WYP6
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