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Mopeia virus exonuclease domain fully depleted of manganese un ald compound

Analyse Mopeia virus exonuclease domain fully depleted of manganese un ald compound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SY8
Type: protein
Length: 397 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein
EC: 3.1.13.-
UniProt: Q5S581
Ligands: ZN
Pockets: 6 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleoprotein (EC 3.1.13.-)	protein	198	38% helix, 16% strand	Q5S581
B	Nucleoprotein (EC 3.1.13.-)	protein	199	38% helix, 20% strand	Q5S581

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	218	0.57	0.79	37	empty
2	173	0.47	0.76	21	empty
3	213	0.47	0.74	21	empty
4	91	0.45	0.80	14	empty
5	101	0.39	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 379 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6SY8 · Mopeia Virus Exonuclease domain fully depleted of Manganese un ALD compound · 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 Q5S581
Elsewhere: RCSB PDB 6SY8 · PDBe 6SY8 · UniProt Q5S581

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