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Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase

Analyse Structural and functional analyses of a conserved hydrophobic pocket of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LKZ
Type: protein
Length: 524 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 5
UniProt: Q9Q6P4
Ligands: SFG
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Non-structural protein 5	protein	262	35% helix, 16% strand	Q9Q6P4

Ligands and binding sites

SFG · Sinefungin · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	541	0.69	0.79	60	SFG
2	566	0.68	0.78	60	SFG
3	59	0.48	0.85	18	empty
4	50	0.42	0.83	15	empty

Interfaces

1 interface between chains.

A–B · 149 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3LKZ · Structural and functional analyses of a conserved hydrophobic pocket of 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 Q9Q6P4
Elsewhere: RCSB PDB 3LKZ · PDBe 3LKZ · UniProt Q9Q6P4

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