MolNFT v1 · #106484 · protein

Crystal structure of the autoinhibited dimer of pro-apoptotic bax (I)

4S0O · Apoptosis regulator bax: “Crystal structure of the autoinhibited dimer of pro-apoptotic bax (I)”. X-ray diffraction, 4 pockets (best druggability 0.56). MolNFT v1 #106484 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4S0O
Type: protein
Length: 351 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apoptosis regulator bax
UniProt: Q07812
Pockets: 4 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apoptosis regulator bax	protein	175	75% helix, 0% strand	Q07812
B	Apoptosis regulator bax	protein	176	75% helix, 0% strand	Q07812

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	188	0.56	0.80	28	empty
2	121	0.52	0.81	18	empty
3	123	0.48	0.78	16	empty
4	76	0.32	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 993 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4S0O · Crystal Structure of the Autoinhibited Dimer of Pro-apoptotic BAX (I) · the same entry in another collection · chain A against A, TM-score 1.00
Q07812 · AlphaFold monomer V2.0 prediction for apoptosis regulator bax (Q07812) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q07812
Elsewhere: RCSB PDB 4S0O · PDBe 4S0O · UniProt Q07812

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