Research workbench
Crystal structure of viod hydroxylase in complex with FAD from chromobacterium violaceum. northeast structural genomics consortium target CVR158
Analyse Crystal structure of viod hydroxylase in complex with FAD from chromobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C4A
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable tryptophan hydroxylase viod
- EC
- 1.-.-.-
- UniProt
- Q9S3U8
- Ligands
- FAD
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable tryptophan hydroxylase viod (EC 1.-.-.-) | protein | 365 | 39% helix, 23% strand | Q9S3U8 |
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
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1047 | 0.82 | 0.83 | 98 | FAD |
| 2 | 54 | 0.37 | 0.80 | 19 | empty |
| 3 | 50 | 0.36 | 0.79 | 10 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3C4A · Crystal structure of vioD hydroxylase in complex with FAD from Chromobacterium violaceum.… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9S3U8 · AlphaFold monomer V2.0 prediction for protodeoxyviolaceinate monooxygenase (Q9S3U8) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9S3U8
- Elsewhere: RCSB PDB 3C4A · PDBe 3C4A · UniProt Q9S3U8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.