Research workbench

Human BCL2-A1 in complex with bim-BH3 peptide

Analyse Human BCL2-A1 in complex with bim-BH3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VM6
Type: protein
Length: 169 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BCL-2-related protein A1; BCL-2-like protein 11
UniProt: Q16548, O43521
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BCL-2-related protein A1	protein	144	80% helix, 0% strand	Q16548
B	BCL-2-like protein 11	protein	25	76% helix, 0% strand	O43521

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A, B

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

Interfaces

1 interface between chains.

A–B · 1198 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2VM6 · Human Bcl2-A1 in complex with Bim-BH3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q16548 · AlphaFold monomer V2.0 prediction for BCL-2-related protein A1 (Q16548) · a predicted model of the same protein · chain A against A, TM-score 0.96
O43521 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 11 (O43521) · a predicted model of the same protein · chain B against A, TM-score 0.64

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 Q16548
Every structure of UniProt O43521
Elsewhere: RCSB PDB 2VM6 · PDBe 2VM6 · UniProt Q16548 · UniProt O43521

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