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Structural and biochemical characterization of endoribonuclease NSP15 encoded by middle east respiratory syndrome coronavirus

Analyse Structural and biochemical characterization of endoribonuclease NSP15 encoded… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YVD
Type: protein
Length: 682 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NSP15
UniProt: A0A0U2GPI9
Pockets: 4 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	NSP15	protein	341	21% helix, 30% strand	A0A0U2GPI9

Ligands and binding sites

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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	285	0.59	0.78	37	empty
2	191	0.58	0.81	30	empty
3	201	0.57	0.80	31	empty
4	83	0.31	0.73	23	empty

Interfaces

1 interface between chains.

A–B · 355 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

5YVD · Structural and biochemical characterization of endoribonuclease Nsp15 encoded by Middle… · 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 A0A0U2GPI9
Elsewhere: RCSB PDB 5YVD · PDBe 5YVD · UniProt A0A0U2GPI9

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