Research workbench
Structure of the tetracycline degrading monooxygenase TETX2 from bacteroides thetaiotaomicron
Analyse Structure of the tetracycline degrading monooxygenase TETX2 from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XDO
- Type
- protein
- Length
- 1,462 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q93L51
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 367 | — | Q93L51 |
| B | — | protein | 366 | — | Q93L51 |
| C | — | protein | 365 | — | Q93L51 |
| D | — | protein | 364 | — | Q93L51 |
Compared structures
- 2XDO · Structure of the Tetracycline degrading Monooxygenase TetX2 from Bacteroides… · the same entry in another collection · chain D against D, TM-score 1.00
- Q93L51 · AlphaFold monomer V2.0 prediction for flavin-dependent monooxygenase (Q93L51) · a predicted model of the same protein · chain D 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 Q93L51
- Elsewhere: RCSB PDB 2XDO · PDBe 2XDO · UniProt Q93L51
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