MolNFT v1 · #135284 · protein
Crystal structure of tetracycline destructase TET(56)
5TUM: “Crystal structure of tetracycline destructase TET(56)”. X-ray diffraction, 1 ligand (FAD), 4 pockets (best druggability 0.84). MolNFT v1 #135284 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TUM
- Type
- protein
- Length
- 731 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetracycline destructase TET(56)
- UniProt
- D3HKY4
- Ligands
- FAD
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetracycline destructase TET(56) | protein | 369 | 35% helix, 27% strand | D3HKY4 |
| B | Tetracycline destructase TET(56) | protein | 362 | 35% helix, 28% strand | D3HKY4 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 991 | 0.84 | 0.85 | 101 | FAD |
| 2 | 1129 | 0.81 | 0.83 | 94 | FAD |
| 3 | 124 | 0.41 | 0.75 | 22 | empty |
| 4 | 73 | 0.38 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 283 Ų buried · 0 hydrogen bonds · protein-protein
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 D3HKY4
- Elsewhere: RCSB PDB 5TUM · PDBe 5TUM · UniProt D3HKY4
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