MolNFT v1 · #70472 · protein
Sulfhydryl oxidase fragment of human QSOX1
3LLK · Sulfhydryl oxidase 1: “Sulfhydryl oxidase fragment of human QSOX1”. X-ray diffraction, 1 ligand (FAD), 4 pockets (best druggability 0.87). MolNFT v1 #70472 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LLK
- Type
- protein
- Length
- 725 residues
- Chains
- 3
- 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
- 4 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 61% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfhydryl oxidase 1 (EC 1.8.3.2) | protein | 241 | 61% helix, 5% strand | O00391 |
| B | Sulfhydryl oxidase 1 (EC 1.8.3.2) | protein | 243 | 61% helix, 5% strand | O00391 |
| C | Sulfhydryl oxidase 1 (EC 1.8.3.2) | protein | 241 | 60% helix, 4% strand | O00391 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 3 copies · chains A, B, C
- FLC · Citrate anion · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1198 | 0.87 | 0.88 | 127 | FAD |
| 2 | 1064 | 0.82 | 0.83 | 106 | FAD |
| 3 | 112 | 0.40 | 0.76 | 23 | empty |
| 4 | 89 | 0.36 | 0.75 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 933 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 669 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 253 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 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 3LLK · PDBe 3LLK · UniProt O00391
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.