MolNFT v1 · #139595 · protein
Crystal structure of baculoviral sulfhydryl oxidase ACP33 (wide type)
5XKI · FAD-linked sulfhydryl oxidase: “Crystal structure of baculoviral sulfhydryl oxidase ACP33 (wide type)”. X-ray diffraction, 1 ligand (FAD), 13 pockets (best druggability 0.80). MolNFT v1 #139595 on GenesisL1: 3D structure, binding…
- PDB
- 5XKI
- Type
- protein
- Length
- 512 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAD-linked sulfhydryl oxidase
- EC
- 1.8.3.2
- UniProt
- P41480
- Ligands
- FAD
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-linked sulfhydryl oxidase (EC 1.8.3.2) | protein | 253 | 65% helix, 2% strand | P41480 |
| B | FAD-linked sulfhydryl oxidase (EC 1.8.3.2) | protein | 259 | 67% helix, 2% strand | P41480 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.80 | 0.96 | 32 | empty |
| 2 | 139 | 0.80 | 0.97 | 28 | empty |
| 3 | 129 | 0.61 | 0.84 | 17 | FAD |
| 4 | 116 | 0.60 | 0.85 | 18 | FAD |
| 5 | 66 | 0.55 | 0.87 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2082 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5XKI · Crystal structure of baculoviral sulfhydryl oxidase AcP33 (wide type) · 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 5XKI · PDBe 5XKI · UniProt P41480
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