Research workbench

BCL-2 complex with beclin 1 BH3 domain

Analyse BCL-2 complex with beclin 1 BH3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VAU
Type: protein
Length: 645 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P10415, Q14457

Structure

x-ray diffraction · 7 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	151	—	P10415
B	—	protein	137	—	P10415
C	—	protein	139	—	P10415
D	—	protein	137	—	P10415
E	—	protein	20	—	Q14457
G, H	—	protein	20	—	Q14457
F	—	protein	21	—	Q14457

Compared structures

5VAU · Bcl-2 complex with Beclin 1 BH3 domain · the same entry in another collection · chain H against H, 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 0.97

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
Every structure of UniProt Q14457
Elsewhere: RCSB PDB 5VAU · PDBe 5VAU · UniProt P10415 · UniProt Q14457

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