MolNFT v1 · #87034 · protein

Structure of herpesvirus fusion glycoprotein B-bilayer complex revealing the protein-membrane and lateral protein-protein interaction

4BOM · Envelope glycoprotein B: “Structure of herpesvirus fusion glycoprotein B-bilayer complex revealing the protein-membrane and lateral…”. Electron microscopy, 20 pockets (best druggability 0.84). MolNFT v1 #87034 on GenesisL1: 3D…

PDB: 4BOM
Type: protein
Length: 1,821 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope glycoprotein B
UniProt: P06437
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 22% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Envelope glycoprotein B	protein	607	22% helix, 34% strand	P06437

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	806	0.84	0.86	73	empty
2	982	0.80	0.82	109	empty
3	914	0.80	0.82	86	empty
4	759	0.77	0.81	86	empty
5	622	0.70	0.79	66	empty

Interfaces

3 interfaces between chains.

B–C · 5420 Å² buried · 72 hydrogen bonds · protein-protein
A–C · 5412 Å² buried · 70 hydrogen bonds · protein-protein
A–B · 5314 Å² buried · 80 hydrogen bonds · protein-protein

Compared structures

4BOM · Structure of herpesvirus fusion glycoprotein B-bilayer complex revealing the… · 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 P06437
Elsewhere: RCSB PDB 4BOM · PDBe 4BOM · UniProt P06437

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