MolNFT v2 · #98600 · protein
FAD-linked sulfhydryl oxidase ALR mutation
4LDK: “FAD-linked sulfhydryl oxidase ALR mutation”. X-ray diffraction at 2.04, 2 ligands (FAD, NA), 1 pocket (best druggability 0.63). MolNFT v2 #98600 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4LDK
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.04
- Source
- Homo sapiens
- Molecule
- FAD-linked sulfhydryl oxidase ALR
- EC
- 1.8.3.2
- UniProt
- P55789
- Ligands
- FAD, NA
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · resolution 2.04 · 1 distinct chain · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-linked sulfhydryl oxidase ALR (EC 1.8.3.2) | protein | 115 | 65% helix, 0% strand | P55789 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 214 | 0.63 | 0.82 | 30 | FAD, NA |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, oxidation).
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 P55789
- Elsewhere: RCSB PDB 4LDK · PDBe 4LDK · UniProt P55789
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.