MolNFT v1 · #160822 · protein

Crystal structure of ligand free phqk

6PVG · FAD monooxygenase: “Crystal structure of ligand free phqk”. X-ray diffraction, 1 ligand (FAD), 4 pockets (best druggability 0.83). MolNFT v1 #160822 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6PVG
Type: protein
Length: 445 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAD monooxygenase
UniProt: L0E4H0
Ligands: FAD
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAD monooxygenase	protein	445	36% helix, 24% strand	L0E4H0

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

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	779	0.83	0.86	89	FAD
2	127	0.46	0.78	26	empty
3	83	0.32	0.74	19	empty
4	52	0.29	0.76	12	empty

Compared structures

6PVG · Crystal structure of ligand free PhqK · 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 6PVG · PDBe 6PVG · UniProt L0E4H0

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