Research workbench
Mandelate oxidase mutant-Y128F with the C4A-oh-FMN adduct
Analyse Mandelate oxidase mutant-Y128F with the C4A-oh-FMN adduct in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AI7
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxymandelate oxidase
- EC
- 1.1.3.46
- UniProt
- O52792
- Ligands
- 9Q6
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxymandelate oxidase (EC 1.1.3.46) | protein | 329 | 44% helix, 14% strand | O52792 |
Ligands and binding sites
- 9Q6 · 1-deoxy-1-[(4AS)-4A-hydroxy-7,8-dimethyl-2,4-dioxo-3,4, 4A,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-5-O-phosphono-D-ribitol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.75 | 0.86 | 46 | 9Q6 |
| 2 | 53 | 0.31 | 0.76 | 12 | empty |
| 3 | 63 | 0.30 | 0.74 | 13 | empty |
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 O52792
- Elsewhere: RCSB PDB 6AI7 · PDBe 6AI7 · UniProt O52792
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