Research workbench

BAK L100A

Analyse BAK L100A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VX1
Type: protein
Length: 326 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BCL-2 homologous ANTAGONIST/KILLER
UniProt: Q16611
Pockets: 5 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BCL-2 homologous ANTAGONIST/KILLER	protein	163	68% helix, 0% strand	Q16611
B	BCL-2 homologous ANTAGONIST/KILLER	protein	163	73% helix, 0% strand	Q16611

Pockets

5 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	153	0.48	0.77	23	empty
2	85	0.42	0.79	20	empty
3	89	0.41	0.78	21	empty
4	83	0.34	0.75	21	empty
5	60	0.30	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 495 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5VX1 · Bak L100A · 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 A against A, TM-score 0.91

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 Q16611
Elsewhere: RCSB PDB 5VX1 · PDBe 5VX1 · UniProt Q16611

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