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Epstein-barr virus protease

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

PDB: 1O6E
Type: protein
Length: 457 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein P40
EC: 3.4.21.97
UniProt: P03234
Ligands: ISP
Pockets: 7 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein P40 (EC 3.4.21.97)	protein	225	32% helix, 23% strand	P03234
B	Capsid protein P40 (EC 3.4.21.97)	protein	232	30% helix, 22% strand	P03234

Ligands and binding sites

ISP · Phosphorylisopropane · ligand · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	262	0.53	0.76	38	ISP
2	247	0.51	0.75	43	ISP
3	106	0.51	0.81	18	empty
4	67	0.49	0.84	17	empty
5	80	0.42	0.80	15	empty

Interfaces

1 interface between chains.

A–B · 1358 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

1O6E · Epstein-Barr virus protease · 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 P03234
Elsewhere: RCSB PDB 1O6E · PDBe 1O6E · UniProt P03234

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