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Crystal structure and mutational analysis of the endoribonuclease from human coronavirus 229E

Analyse Crystal structure and mutational analysis of the endoribonuclease from human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4RS4
Type
protein
Length
2,042 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uridylate-specific endoribonuclease
EC
3.1.-.-
UniProt
P0C6X1
Pockets
20 · best druggability 0.84

Structure

x-ray diffraction · 5 distinct chains · 20% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, EUridylate-specific endoribonuclease (EC 3.1.-.-)protein34119% helix, 30% strandP0C6X1
BUridylate-specific endoribonuclease (EC 3.1.-.-)protein34518% helix, 32% strandP0C6X1
CUridylate-specific endoribonuclease (EC 3.1.-.-)protein33220% helix, 30% strandP0C6X1
DUridylate-specific endoribonuclease (EC 3.1.-.-)protein33719% helix, 31% strandP0C6X1
FUridylate-specific endoribonuclease (EC 3.1.-.-)protein34621% helix, 34% strandP0C6X1

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13380.840.9333empty
27060.830.8776empty
33930.810.9042empty
46460.810.8669empty
58310.790.82109empty

Interfaces

12 interfaces between chains.

  • E–F · 1313 Ų buried · 14 hydrogen bonds · protein-protein
  • A–D · 1285 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 1269 Ų buried · 14 hydrogen bonds · protein-protein
  • B–F · 1258 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 1254 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 4RS4 · Crystal structure and mutational analysis of the endoribonuclease from human coronavirus… · the same entry in another collection · chain A against A, TM-score 1.00

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