Research workbench
Crysal structure of the mimivirus sulfhydryl oxidase R596
Analyse Crysal structure of the mimivirus sulfhydryl oxidase R596 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TD7
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAD-linked sulfhydryl oxidase R596
- EC
- 1.8.3.2
- UniProt
- Q5UP54
- Ligands
- FAD
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 65% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-linked sulfhydryl oxidase R596 (EC 1.8.3.2) | protein | 253 | 65% helix, 1% strand | Q5UP54 |
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
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 757 | 0.79 | 0.82 | 75 | FAD |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3TD7 · Crysal structure of the mimivirus sulfhydryl oxidase R596 · 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 Q5UP54
- Elsewhere: RCSB PDB 3TD7 · PDBe 3TD7 · UniProt Q5UP54
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