Research workbench
Crystal structure of phqk in complex with paraherquamide K
Analyse Crystal structure of phqk in complex with paraherquamide K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PVH
- Type
- protein
- Length
- 444 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAD monooxygenase
- UniProt
- L0E4H0
- Ligands
- OZ4, FAD
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD monooxygenase | protein | 444 | 37% helix, 24% strand | L0E4H0 |
Ligands and binding sites
- OZ4 · (7as,12s,12ar,13as)-3,3,12,14,14-pentamethyl-3,7,11,12, 13,13A,14,15-octahydro-8H,10H-7A,12A-(epiminomethano) indolizino[6,7-h]pyrano[3,2-a]carbazol-16-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
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1042 | 0.86 | 0.86 | 91 | OZ4, FAD |
| 2 | 206 | 0.52 | 0.77 | 48 | empty |
| 3 | 102 | 0.42 | 0.77 | 25 | empty |
| 4 | 81 | 0.34 | 0.75 | 20 | empty |
| 5 | 58 | 0.29 | 0.75 | 14 | empty |
Compared structures
- 6PVH · Crystal structure of PhqK in complex with paraherquamide K · 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 6PVH · PDBe 6PVH · UniProt L0E4H0
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