Research workbench
Salicylate hydroxylase substrate complex
Analyse Salicylate hydroxylase substrate complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EVY
- Type
- protein
- Length
- 411 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Salicylate hydroxylase
- EC
- 1.14.13.1
- UniProt
- Q59713
- Ligands
- FAD, SAL
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Salicylate hydroxylase (EC 1.14.13.1) | protein | 411 | 35% helix, 24% strand | Q59713 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains X
- SAL · 2-hydroxybenzoic acid · ligand · chains X
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 | 643 | 0.78 | 0.83 | 60 | FAD, SAL |
| 2 | 108 | 0.42 | 0.78 | 19 | empty |
| 3 | 91 | 0.41 | 0.78 | 16 | empty |
Compared structures
- 5EVY · Salicylate hydroxylase substrate complex · the same entry in another collection · chain X against X, 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 Q59713
- Elsewhere: RCSB PDB 5EVY · PDBe 5EVY · UniProt Q59713
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