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Structure of a BCL-W dimer

Analyse Structure of a BCL-W dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Y6W
Type: protein
Length: 293 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BCL-2-like protein 2
UniProt: Q92843
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BCL-2-like protein 2	protein	146	79% helix, 0% strand	Q92843
B	BCL-2-like protein 2	protein	147	76% helix, 0% strand	Q92843

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, B
PGE · Triethylene glycol · additive · chains A, 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1010	0.72	0.75	52	PEG, PGE

Interfaces

1 interface between chains.

A–B · 1877 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

2Y6W · Structure of a Bcl-w dimer · the same entry in another collection · chain A against A, TM-score 1.00
Q92843 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 2 (Q92843) · a predicted model of the same protein · chain B against A, TM-score 0.76

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 Q92843
Elsewhere: RCSB PDB 2Y6W · PDBe 2Y6W · UniProt Q92843

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