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Crystal structure of ebinur lake virus cap snatching endonuclease (N52A mutant)

Analyse Crystal structure of ebinur lake virus cap snatching endonuclease (N52A mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EWW
Type: protein
Length: 345 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Replicase
EC: 2.7.7.48
UniProt: A0A059WLS9
Ligands: MN
Pockets: 2 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Replicase (EC 2.7.7.48)	protein	174	51% helix, 14% strand	A0A059WLS9
B	Replicase (EC 2.7.7.48)	protein	171	52% helix, 14% strand	A0A059WLS9

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.31	0.75	18	empty
2	77	0.29	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 468 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7EWW · Crystal structure of Ebinur Lake virus cap snatching endonuclease (N52A mutant) · 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 A0A059WLS9
Elsewhere: RCSB PDB 7EWW · PDBe 7EWW · UniProt A0A059WLS9

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