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Crystal structure of NSP10 from SARS coronavirus

Analyse Crystal structure of NSP10 from SARS coronavirus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FYG
Type
protein
Length
128 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Replicase polyprotein 1AB
UniProt
Q6JH39
Ligands
ZN
Pockets
1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReplicase polyprotein 1ABprotein12829% helix, 13% strandQ6JH39

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11300.460.7718empty

Compared structures

  • 2FYG · Crystal structure of NSP10 from Sars coronavirus · the same entry in another collection · chain A against A, TM-score 1.00

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