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The structure of vaccinia virus N1

Analyse The structure of vaccinia virus N1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2UXE
Type: protein
Length: 684 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein
UniProt: Q49PX0
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Hypothetical protein	protein	114	78% helix, 0% strand	Q49PX0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	581	0.63	0.75	58	empty
2	600	0.62	0.74	58	empty
3	160	0.44	0.75	21	empty
4	138	0.44	0.76	21	empty

Interfaces

5 interfaces between chains.

D–F · 1037 Å² buried · 21 hydrogen bonds · protein-protein
A–C · 1029 Å² buried · 22 hydrogen bonds · protein-protein
B–E · 1028 Å² buried · 25 hydrogen bonds · protein-protein
C–E · 681 Å² buried · 13 hydrogen bonds · protein-protein
A–F · 671 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 42 modified (engineered).

Compared structures

2UXE · The structure of Vaccinia virus N1 · 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 Q49PX0
Elsewhere: RCSB PDB 2UXE · PDBe 2UXE · UniProt Q49PX0

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