MolNFT v1 · #180996 · protein

Crystal structure of BCL-2 in complex with prodrug abbv-167

7LHB · Apoptosis regulator BCL-2: “Crystal structure of BCL-2 in complex with prodrug abbv-167”. X-ray diffraction, 1 ligand (XZD), 5 pockets (best druggability 0.65). MolNFT v1 #180996 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 7LHB
Type: protein
Length: 403 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apoptosis regulator BCL-2
UniProt: P10415
Ligands: XZD
Pockets: 5 · best druggability 0.65

Structure

x-ray diffraction · 3 distinct chains · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apoptosis regulator BCL-2	protein	137	78% helix, 0% strand	P10415
B	Apoptosis regulator BCL-2	protein	136	78% helix, 0% strand	P10415
C	Apoptosis regulator BCL-2	protein	130	76% helix, 0% strand	P10415

Ligands and binding sites

XZD · Phosphoric acid mono-[5-(5-{4-[2-(4-chloro-phenyl)-4,4-dimethyl-cyclohex-1-enylmethyl]-piperazin-1-yl}-2-{3-nitro-4-[(tetrahydro-pyran-4-ylmethyl)-amino]-benzenesulfonylaminocarbonyl}-phenoxy)-pyrrolo[2,3-b]pyridin-7-ylmethyl] ester · ligand · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	552	0.65	0.76	43	empty
2	133	0.48	0.78	15	empty
3	110	0.46	0.78	12	empty
4	147	0.43	0.75	20	XZD
5	50	0.26	0.73	12	empty

Interfaces

2 interfaces between chains.

A–B · 215 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 204 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7LHB · Crystal structure of Bcl-2 in complex with prodrug ABBV-167 · the same entry in another collection · chain A against A, TM-score 1.00
P10415 · AlphaFold monomer V2.0 prediction for apoptosis regulator BCL-2 (P10415) · a predicted model of the same protein · chain C against A, TM-score 0.98

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 P10415
Elsewhere: RCSB PDB 7LHB · PDBe 7LHB · UniProt P10415

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