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Crystal structure of Bcl-2 in complex with HBx-BH3 motif

Analyse Crystal structure of Bcl-2 in complex with HBx-BH3 motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FCG
Type: protein
Length: 176 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.1
Source: Homo sapiens; SYNTHETIC CONSTRUCT
Molecule: Apoptosis regulator Bcl-2; Protein X
UniProt: E9L5H4
Pockets: 1 · best druggability 0.24

Structure

x-ray diffraction · resolution 2.1 · 2 distinct chains · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apoptosis regulator Bcl-2	protein	150	73% helix, 0% strand	—
C	Protein X	protein	26	62% helix, 0% strand	E9L5H4

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.24	0.73	14	empty

Interfaces

1 interface between chains.

A–C · 1240 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

5FCG · Crystal structure of BCL-2 in complex with hbx-BH3 motif · the same entry in another collection · chain A against A, TM-score 1.00

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 E9L5H4
Elsewhere: RCSB PDB 5FCG · PDBe 5FCG · UniProt E9L5H4

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