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1.2 A resolution structure of human hydroxyacid oxidase 1 bound with FMN and 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole
Analyse 1.2 A resolution structure of human hydroxyacid oxidase 1 bound with FMN and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GMC
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.2
- Source
- Homo sapiens
- Molecule
- Hydroxyacid oxidase 1
- EC
- 1.1.3.15
- UniProt
- Q9UJM8
- Ligands
- FMN, C7C
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · resolution 1.2 · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxyacid oxidase 1 (EC 1.1.3.15) | protein | 360 | 45% helix, 14% strand | Q9UJM8 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- C7C · 5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole-4-carboxylate · ligand · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · 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 | 205 | 0.83 | 0.97 | 41 | FMN, C7C |
| 2 | 139 | 0.47 | 0.77 | 26 | empty |
| 3 | 65 | 0.29 | 0.73 | 14 | empty |
Compared structures
- 6GMC · 1.2 a resolution structure of human hydroxyacid oxidase 1 bound with FMN and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UJM8 · AlphaFold monomer V2.0 prediction for hydroxyacid oxidase 1 (Q9UJM8) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9UJM8
- Elsewhere: RCSB PDB 6GMC · PDBe 6GMC · UniProt Q9UJM8
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