MolNFT v1 · #76941 · protein
Structure of baculovirus sulfhydryl oxidase AC92
3QZY: “Structure of baculovirus sulfhydryl oxidase AC92”. X-ray diffraction, 2 ligands (FAD, PO4), 13 pockets (best druggability 0.67). MolNFT v1 #76941 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3QZY
- Type
- protein
- Length
- 487 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baculovirus sulfhydryl oxidase AC92
- EC
- 1.8.3.2
- UniProt
- P41480
- Ligands
- FAD, PO4
- Pockets
- 13 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Baculovirus sulfhydryl oxidase AC92 (EC 1.8.3.2) | protein | 240 | 68% helix, 3% strand | P41480 |
| B | Baculovirus sulfhydryl oxidase AC92 (EC 1.8.3.2) | protein | 247 | 68% helix, 2% strand | P41480 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 376 | 0.67 | 0.80 | 43 | FAD |
| 2 | 67 | 0.64 | 0.92 | 23 | empty |
| 3 | 200 | 0.62 | 0.82 | 32 | FAD |
| 4 | 76 | 0.60 | 0.89 | 20 | empty |
| 5 | 293 | 0.57 | 0.77 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1264 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3QZY · Structure of Baculovirus Sulfhydryl Oxidase Ac92 · the same entry in another collection · chain A against A, TM-score 1.00
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 P41480
- Elsewhere: RCSB PDB 3QZY · PDBe 3QZY · UniProt P41480
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