Research workbench
Crystal structure of tetracycline destructase TET(51)
Analyse Crystal structure of tetracycline destructase TET(51) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TUK
- Type
- protein
- Length
- 1,476 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetracycline destructase TET(51)
- UniProt
- A0A0H4TFU4
- Ligands
- FAD
- Pockets
- 12 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetracycline destructase TET(51) | protein | 372 | 36% helix, 27% strand | A0A0H4TFU4 |
| B | Tetracycline destructase TET(51) | protein | 373 | 37% helix, 27% strand | A0A0H4TFU4 |
| C | Tetracycline destructase TET(51) | protein | 367 | 36% helix, 27% strand | A0A0H4TFU4 |
| D | Tetracycline destructase TET(51) | protein | 364 | 37% helix, 28% strand | A0A0H4TFU4 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 976 | 0.84 | 0.85 | 105 | GOL, FAD |
| 2 | 1013 | 0.83 | 0.84 | 98 | GOL, FAD |
| 3 | 987 | 0.83 | 0.84 | 91 | GOL, FAD |
| 4 | 992 | 0.83 | 0.84 | 98 | GOL, FAD |
| 5 | 682 | 0.65 | 0.75 | 49 | empty |
Interfaces
4 interfaces between chains.
- B–C · 879 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 788 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 378 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 319 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5TUK · Crystal structure of tetracycline destructase Tet(51) · the same entry in another collection · chain D against D, 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 A0A0H4TFU4
- Elsewhere: RCSB PDB 5TUK · PDBe 5TUK · UniProt A0A0H4TFU4
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