Research workbench
Human aldehyde oxidase SNP G1269R
Analyse Human aldehyde oxidase SNP G1269R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q6Q
- Type
- protein
- Length
- 1,292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldehyde oxidase
- EC
- 1.2.3.1, 1.17.3.-
- UniProt
- Q06278
- Ligands
- FES, FAD
- Pockets
- 16 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldehyde oxidase (EC 1.2.3.1, 1.17.3.-) | protein | 1292 | 33% helix, 23% strand | Q06278 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- MLI · Malonate ion · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1084 | 0.85 | 0.86 | 93 | FAD, MLI |
| 2 | 900 | 0.82 | 0.84 | 100 | MLI |
| 3 | 553 | 0.82 | 0.88 | 52 | empty |
| 4 | 736 | 0.79 | 0.83 | 66 | MLI |
| 5 | 674 | 0.73 | 0.80 | 70 | 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 Q06278
- Elsewhere: RCSB PDB 6Q6Q · PDBe 6Q6Q · UniProt Q06278
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