Research workbench
Crystal structure of hydroquinone 1,2-dioxygenase from sphingomonas sp. TTNP3 with 4-hydroxybenzoate bound
Analyse Crystal structure of hydroquinone 1,2-dioxygenase from sphingomonas sp. TTNP3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M21
- Type
- protein
- Length
- 1,976 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F8TW82, F8TW83
- Ligands
- PHB, FE
Structure
x-ray diffraction · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 166 | — | F8TW82 |
| B | — | protein | 325 | — | F8TW83 |
| C, E | — | protein | 167 | — | F8TW82 |
| D | — | protein | 327 | — | F8TW83 |
| F | — | protein | 326 | — | F8TW83 |
| G | — | protein | 165 | — | F8TW82 |
| H | — | protein | 333 | — | F8TW83 |
Ligands and binding sites
- PHB · P-hydroxybenzoic acid · ligand · 4 copies · chains B, D, F, H
- FE · Fe (III) ion · metal · 4 copies · chains B, D, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5M21 · Crystal structure of hydroqui 1,2-dioxygenase from Sphingomonas sp. TTNP3 with… · 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 F8TW82
- Every structure of UniProt F8TW83
- Elsewhere: RCSB PDB 5M21 · PDBe 5M21 · UniProt F8TW82 · UniProt F8TW83
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.