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Crystal structure of pseudorabies virus glycoprotein B

Analyse Crystal structure of pseudorabies virus glycoprotein B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ESC
Type: protein
Length: 594 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope glycoprotein B
UniProt: G3G8X1
Ligands: NAG
Pockets: 5 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Envelope glycoprotein B	protein	594	20% helix, 37% strand	G3G8X1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
GOL · Glycerol · additive · chains A

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

Pockets

5 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	209	0.52	0.77	28	empty
2	141	0.50	0.79	31	GOL
3	67	0.42	0.81	19	empty
4	98	0.38	0.75	20	empty
5	89	0.32	0.73	21	empty

Modifications

Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

6ESC · Crystal structure of Pseudorabies virus glycoprotein B · 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 G3G8X1
Elsewhere: RCSB PDB 6ESC · PDBe 6ESC · UniProt G3G8X1

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