MolNFT v1 · #70471 · protein
Sulfhydryl oxidase fragment of human QSOX1
3LLI · Sulfhydryl oxidase 1: “Sulfhydryl oxidase fragment of human QSOX1”. X-ray diffraction, 1 ligand (FAD), 2 pockets (best druggability 0.80). MolNFT v1 #70471 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LLI
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfhydryl oxidase 1
- EC
- 1.8.3.2
- UniProt
- O00391
- Ligands
- FAD
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfhydryl oxidase 1 (EC 1.8.3.2) | protein | 251 | 62% helix, 6% strand | O00391 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · 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 | 553 | 0.80 | 0.86 | 54 | FAD |
| 2 | 53 | 0.40 | 0.81 | 18 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 O00391
- Elsewhere: RCSB PDB 3LLI · PDBe 3LLI · UniProt O00391
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