Research workbench

Vaccinia virus F1L bound to bak BH3

Analyse Vaccinia virus F1L bound to bak BH3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4D2L
Type: protein
Length: 161 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein F1L; BCL-2 homologous ANTAGONIST/KILLER
UniProt: O57173, Q16611
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein F1L	protein	138	79% helix, 0% strand	O57173
B	BCL-2 homologous ANTAGONIST/KILLER	protein	23	70% helix, 0% strand	Q16611

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	228	0.49	0.74	23	empty
2	143	0.46	0.76	18	empty
3	123	0.37	0.73	19	empty

Interfaces

1 interface between chains.

A–B · 900 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4D2L · Vaccinia Virus F1L bound to Bak BH3 · the same entry in another collection · chain A against A, TM-score 1.00
Q16611 · AlphaFold monomer V2.0 prediction for BCL-2 homologous ANTAGONIST/KILLER (Q16611) · a predicted model of the same protein · chain B against A, TM-score 0.70

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 O57173
Every structure of UniProt Q16611
Elsewhere: RCSB PDB 4D2L · PDBe 4D2L · UniProt O57173 · UniProt Q16611

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.