Research workbench

Crystal structure of the postfusion form of baculovirus fusion protein GP64

Analyse Crystal structure of the postfusion form of baculovirus fusion protein GP64 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DUZ
Type: protein
Length: 418 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major envelope glycoprotein
UniProt: P17501
Ligands: HG
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Major envelope glycoprotein	protein	418	22% helix, 33% strand	P17501

Ligands and binding sites

HG · Mercury (II) ion · metal · 5 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	87	0.36	0.76	15	empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

3DUZ · Crystal structure of the postfusion form of baculovirus fusion protein GP64 · 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 P17501
Elsewhere: RCSB PDB 3DUZ · PDBe 3DUZ · UniProt P17501

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