Research workbench
Crystal structure of phqk in complex with paraherquamide L
Analyse Crystal structure of phqk in complex with paraherquamide L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PVI
- Type
- protein
- Length
- 438 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAD monooxygenase
- UniProt
- L0E4H0
- Ligands
- OZ7, FAD
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD monooxygenase | protein | 438 | 38% helix, 24% strand | L0E4H0 |
Ligands and binding sites
- OZ7 · (8as,13s,13ar,14as)-4,4,13,15,15-pentamethyl-12,13,14, 14A,15,16-hexahydro-4H,8H,9H,11H-8A,13A-(epiminomethano)[1,4]dioxepino[2,3-a]indolizino[6,7-h]carbazol-17-one · ligand · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 978 | 0.86 | 0.87 | 100 | OZ7, FAD |
| 2 | 145 | 0.61 | 0.85 | 31 | empty |
| 3 | 107 | 0.41 | 0.77 | 27 | empty |
| 4 | 62 | 0.39 | 0.80 | 15 | empty |
| 5 | 101 | 0.38 | 0.75 | 22 | empty |
Compared structures
- 6PVI · Crystal structure of PhqK in complex with paraherquamide L · the same entry in another collection · chain A against A, TM-score 1.00
- L0E4H0 · AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase phqk (L0E4H0) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 L0E4H0
- Elsewhere: RCSB PDB 6PVI · PDBe 6PVI · UniProt L0E4H0
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