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Crystal structure of epstein-barr virus nuclear antigen-1, EBNA1, bound to fragment

Analyse Crystal structure of epstein-barr virus nuclear antigen-1, EBNA1, bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VH6
Type: protein
Length: 275 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epstein-barr nuclear antigen 1
UniProt: P03211
Ligands: QX4
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epstein-barr nuclear antigen 1	protein	141	34% helix, 27% strand	P03211
B	Epstein-barr nuclear antigen 1	protein	134	34% helix, 28% strand	P03211

Ligands and binding sites

QX4 · 4-hydroxy-6-methyl-2H-1-benzopyran-2-one · ligand · chains B

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	54	0.39	0.81	14	QX4

Interfaces

1 interface between chains.

A–B · 2006 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

6VH6 · Crystal structure of Epstein-Barr Virus Nuclear Antigen-1, EBNA1, bound to fragment · 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 P03211
Elsewhere: RCSB PDB 6VH6 · PDBe 6VH6 · UniProt P03211

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