Research workbench
Mandelate oxidase with the 2-hydroxy-3-oxosuccinic acid
Analyse Mandelate oxidase with the 2-hydroxy-3-oxosuccinic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BSR
- Type
- protein
- Length
- 330 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
- F7F, F7C
- Pockets
- 2 · best druggability 0.76
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 | 330 | 44% helix, 14% strand | O52792 |
Ligands and binding sites
- F7F · 3-pyridin-4-yl-2,4-dihydro-indeno[1,2-.c.]pyrazole · ligand · chains A
- F7C · (2~{S})-2-oxidanyl-3-oxidanylidene-butanedioic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 355 | 0.76 | 0.87 | 56 | F7F, F7C |
| 2 | 104 | 0.36 | 0.74 | 24 | empty |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 7BSR · PDBe 7BSR · UniProt O52792
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