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The crystal structure of mandelate oxidase Y128F with 3,3-difluoro-2, 2-dihydroxy-3-phenylpropionic acid
Analyse The crystal structure of mandelate oxidase Y128F with 3,3-difluoro-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A01
- Type
- protein
- Length
- 333 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
- FMN, 9NO
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxymandelate oxidase (EC 1.1.3.46) | protein | 333 | 45% helix, 15% strand | O52792 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- 9NO · 3,3-difluoro-2,2-dihydroxy-3-phenylpropanoic acid · 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 | 325 | 0.77 | 0.87 | 43 | FMN, 9NO |
| 2 | 113 | 0.40 | 0.75 | 23 | empty |
| 3 | 65 | 0.30 | 0.75 | 16 | 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 6A01 · PDBe 6A01 · UniProt O52792
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