Research workbench
Crystal structure of azoreductase azrc in complex with sulfone- modified azo dye orange I
Analyse Crystal structure of azoreductase azrc in complex with sulfone- modified azo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3W79
- Type
- protein
- Length
- 840 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN-dependent NADH-azoreductase
- EC
- 1.7.-.-
- UniProt
- C0STY1
- Ligands
- FMN, ORI
- Pockets
- 7 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | FMN-dependent NADH-azoreductase (EC 1.7.-.-) | protein | 210 | 45% helix, 20% strand | C0STY1 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 4 copies · chains A, B, C, D
- ORI · 4-[(E)-(4-hydroxynaphthalen-1-yl)diazenyl]benzenesulfonic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 468 | 0.64 | 0.76 | 45 | FMN, ORI |
| 2 | 289 | 0.61 | 0.79 | 29 | FMN, ORI |
| 3 | 307 | 0.60 | 0.78 | 40 | empty |
| 4 | 379 | 0.59 | 0.75 | 30 | FMN, ORI |
| 5 | 258 | 0.57 | 0.77 | 29 | FMN, ORI |
Interfaces
3 interfaces between chains.
- C–D · 1196 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1193 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 423 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3W79 · Crystal Structure of azoreductase AzrC in complex with sulfone-modified azo dye Orange I · 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 C0STY1
- Elsewhere: RCSB PDB 3W79 · PDBe 3W79 · UniProt C0STY1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.