Research workbench
Crystal structure of baculoviral sulfhydryl oxidase P33 (H114A mutant)
Analyse Crystal structure of baculoviral sulfhydryl oxidase P33 (H114A mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XTO
- Type
- protein
- Length
- 988 residues
- Chains
- 4
- 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
- 20 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-linked sulfhydryl oxidase (EC 1.8.3.2) | protein | 245 | 69% helix, 2% strand | P41480 |
| B | FAD-linked sulfhydryl oxidase (EC 1.8.3.2) | protein | 242 | 70% helix, 2% strand | P41480 |
| C | FAD-linked sulfhydryl oxidase (EC 1.8.3.2) | protein | 250 | 68% helix, 2% strand | P41480 |
| D | FAD-linked sulfhydryl oxidase (EC 1.8.3.2) | protein | 251 | 67% helix, 2% strand | P41480 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 961 | 0.80 | 0.81 | 80 | empty |
| 2 | 875 | 0.75 | 0.79 | 80 | FAD |
| 3 | 231 | 0.75 | 0.89 | 35 | empty |
| 4 | 289 | 0.74 | 0.87 | 38 | empty |
| 5 | 219 | 0.74 | 0.89 | 35 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1719 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1704 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 620 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 428 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 191 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5XTO · Crystal structure of baculoviral sulfhydryl oxidase P33 (H114A mutant) · 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 5XTO · PDBe 5XTO · UniProt P41480
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