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Mutation of mhv coronavirus non-structural protein NSP15 (F307L)

Analyse Mutation of mhv coronavirus non-structural protein NSP15 (F307L) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GTI
Type
protein
Length
348 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Replicase polyprotein 1AB
UniProt
P16342
Ligands
SO4
Pockets
4 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReplicase polyprotein 1ABprotein34821% helix, 29% strandP16342

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 8 copies · chains A
  • GOL · Glycerol · additive · 2 copies · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12600.600.7940empty
21790.500.7730empty
31300.420.7619empty
4600.260.7214empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 2GTI · mutation of MHV coronavirus non-structural protein nsp15 (F307L) · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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