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Atomic structure of the epstein-barr portal, structure I

Analyse Atomic structure of the epstein-barr portal, structure I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RVR
Type: protein
Length: 4,680 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Portal protein
UniProt: A0A0B6VPI0
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 1 distinct chain · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Portal protein	protein	390	52% helix, 12% strand	A0A0B6VPI0

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	1115	0.87	0.88	108	empty
2	1076	0.87	0.88	99	empty
3	1115	0.87	0.88	100	empty
4	1124	0.87	0.88	98	empty
5	1154	0.87	0.88	113	empty

Interfaces

24 interfaces between chains.

J–K · 3448 Å² buried · 19 hydrogen bonds · protein-protein
H–I · 3441 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 3440 Å² buried · 19 hydrogen bonds · protein-protein
G–H · 3437 Å² buried · 19 hydrogen bonds · protein-protein
D–E · 3437 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

6RVR · Atomic structure of the Epstein-Barr portal, structure I · 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 A0A0B6VPI0
Elsewhere: RCSB PDB 6RVR · PDBe 6RVR · UniProt A0A0B6VPI0

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