MolNFT v1 · #135283 · protein
Crystal structure of tetracycline destructase TET(55)
5TUL: “Crystal structure of tetracycline destructase TET(55)”. X-ray diffraction, 1 ligand (PO4), 1 pocket (best druggability 0.80). MolNFT v1 #135283 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TUL
- Type
- protein
- Length
- 377 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetracycline destructase TET(55)
- UniProt
- A0A0H4TXY1
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetracycline destructase TET(55) | protein | 377 | 36% helix, 28% strand | A0A0H4TXY1 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1107 | 0.80 | 0.81 | 97 | PO4 |
Compared structures
- 5TUL · Crystal structure of tetracycline destructase Tet(55) · 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 A0A0H4TXY1
- Elsewhere: RCSB PDB 5TUL · PDBe 5TUL · UniProt A0A0H4TXY1
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