MolNFT v1 · #114096 · protein

Crystal structure of BCL-xl in complex with hbx-BH3 motif

5B1Z · BCL-2-like protein 1: “Crystal structure of BCL-xl in complex with hbx-BH3 motif”. X-ray diffraction, 3 pockets (best druggability 0.64). MolNFT v1 #114096 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5B1Z
Type: protein
Length: 322 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BCL-2-like protein 1; Peptide from protein X
UniProt: Q07817, I3XMW8
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	BCL-2-like protein 1	protein	144	76% helix, 0% strand	Q07817
C	Peptide from protein X	protein	16	50% helix, 0% strand	I3XMW8
D	Peptide from protein X	protein	18	44% helix, 0% strand	I3XMW8

Pockets

3 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	286	0.64	0.81	46	empty
2	125	0.42	0.76	16	empty
3	90	0.37	0.75	16	empty

Interfaces

3 interfaces between chains.

A–B · 2192 Å² buried · 25 hydrogen bonds · protein-protein
B–D · 940 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 937 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

5B1Z · Crystal structure of Bcl-xL in complex with HBx-BH3 motif · the same entry in another collection · chain A against A, TM-score 1.00
Q07817 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 1 (Q07817) · a predicted model of the same protein · chain A against A, TM-score 0.79

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 Q07817
Every structure of UniProt I3XMW8
Elsewhere: RCSB PDB 5B1Z · PDBe 5B1Z · UniProt Q07817 · UniProt I3XMW8

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