MolNFT v1 · #18958 · protein

Solution structure of the BHRF1 protein from epstein-barr virus, a homolog of human BCL-2

1Q59 · Early antigen protein R: “Solution structure of the BHRF1 protein from epstein-barr virus, a homolog of human BCL-2”. Solution nmr, 5 pockets (best druggability 0.74). MolNFT v1 #18958 on GenesisL1: 3D structure, binding sites and…

PDB: 1Q59
Type: protein
Length: 172 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Early antigen protein R
UniProt: P03182
Pockets: 5 · best druggability 0.74

Structure

solution nmr · 1 distinct chain · 53% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Early antigen protein R	protein	172	53% helix, 0% strand	P03182

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	79	0.74	0.97	14	empty
2	123	0.41	0.75	26	empty
3	56	0.39	0.80	10	empty
4	69	0.33	0.75	17	empty
5	64	0.29	0.73	13	empty

Compared structures

1Q59 · Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2 · 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 P03182
Elsewhere: RCSB PDB 1Q59 · PDBe 1Q59 · UniProt P03182

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