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Identification and characterization of novel broad spectrum inhibitors of the flavivirus methyltransferase

Analyse Identification and characterization of novel broad spectrum inhibitors of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CUQ
Type: protein
Length: 514 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nonstructural protein NS5
UniProt: C0LMU0
Ligands: NSC
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nonstructural protein NS5	protein	257	39% helix, 16% strand	C0LMU0

Ligands and binding sites

NSC · N,N'-bis(4-amino-2-methylquinolin-6-yl)urea · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	558	0.65	0.76	60	NSC
2	525	0.64	0.76	57	NSC
3	214	0.52	0.76	32	empty
4	62	0.30	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 366 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5CUQ · Identification and characterization of novel broad spectrum inhibitors of the flavivirus… · the same entry in another collection · chain A against A, 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 C0LMU0
Elsewhere: RCSB PDB 5CUQ · PDBe 5CUQ · UniProt C0LMU0

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