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X-ray structure and activities of an essential mononegavirales L- protein domain

Analyse X-ray structure and activities of an essential mononegavirales L- protein domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4UCI
Type
protein
Length
731 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA-directed RNA polymerase L
UniProt
Q6WB93
Ligands
SAM, GTP, ADN, ZN
Pockets
5 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA-directed RNA polymerase Lprotein36143% helix, 14% strandQ6WB93
BRNA-directed RNA polymerase Lprotein37042% helix, 14% strandQ6WB93

Ligands and binding sites

  • SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
  • GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
  • ADN · Adenosine · ligand · 2 copies · chains A, B
  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • GOL · Glycerol · additive · 7 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16070.670.7768SAM, GTP, GOL
24620.650.7847SAM, GTP
33860.570.7544empty
4520.410.829ADN
5520.300.7715GOL

Interfaces

1 interface between chains.

  • A–B · 655 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4UCI · X-ray structure and activities of an essential Mo gavirales L- protein domain · the same entry in another collection · chain B against B, TM-score 1.00

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