Research workbench

Crystal structure of a trimeric variant of the epstein-barr virus glycoprotein B

Analyse Crystal structure of a trimeric variant of the epstein-barr 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: 3FVC
Type: protein
Length: 559 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoprotein GP110
UniProt: P03188
Ligands: NAG
Pockets: 6 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoprotein GP110	protein	559	19% helix, 36% strand	P03188

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A

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

Pockets

6 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	96	0.44	0.78	18	empty
2	138	0.41	0.74	29	empty
3	85	0.39	0.77	13	empty
4	53	0.31	0.76	13	empty
5	52	0.29	0.75	15	empty

Modifications

Observed in the structure: 4 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

3FVC · Crystal structure of a trimeric variant of the Epstein-Barr 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 P03188
Elsewhere: RCSB PDB 3FVC · PDBe 3FVC · UniProt P03188

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.