Research workbench

Epstein-barr virus, C12 portal dodecamer

Analyse Epstein-barr virus, C12 portal dodecamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BQT
Type: protein
Length: 4,860 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Portal protein
UniProt: P03213
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 50% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, G, I, K, F, H, J, L	Portal protein	protein	405	50% helix, 11% strand	P03213

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	327	0.85	0.95	52	empty
2	291	0.84	0.95	55	empty
3	286	0.84	0.95	50	empty
4	299	0.83	0.94	51	empty
5	609	0.83	0.87	84	empty

Interfaces

24 interfaces between chains.

C–G · 4247 Å² buried · 38 hydrogen bonds · protein-protein
A–K · 4246 Å² buried · 38 hydrogen bonds · protein-protein
B–E · 4242 Å² buried · 34 hydrogen bonds · protein-protein
E–F · 4238 Å² buried · 39 hydrogen bonds · protein-protein
C–J · 4236 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

7BQT · Epstein-Barr virus, C12 portal dodecamer · 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 P03213
Elsewhere: RCSB PDB 7BQT · PDBe 7BQT · UniProt P03213

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