4QVE: Bcl-xL

Crystal structure of Bcl-xL in complex with BID BH3 domain. Determined by X-ray diffraction at 2.05 Å resolution. Released 10 Jun 2015.

Method
X-ray diffraction
Resolution
2.05 Å
Organism
Homo sapiens
Chains
2
Atoms
1,473
Mol. weight
23.08 kDa
Released
10 Jun 2015

Explore 4QVE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QVE contains 10 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix5-1915
α-helix86-10217
α-helix109-1124
α-helix119-13012
α-helix137-15620
α-helix161-17313
α-helix174-1785
α-helix179-1846
α-helix187-1959
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix79-9618

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bcl-2-like protein 1Aprotein169Homo sapiensQ07817 (AlphaFold model)
Peptide from BH3-interacting domain death agonistBprotein34Homo sapiensP55957 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4QVE_1 Bcl-2-like protein 1 (chains A)
MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEAVKQALREAGDEFELR
YRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ
VLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
Sequence of entity 2 (B), FASTA
>4QVE_2 Peptide from BH3-interacting domain death agonist (chains B)
SESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGL

Primary citation

Bh3 induced conformational changes in Bcl-Xl revealed by crystal structure and comparative analysis. Rajan, S., Choi, M., Baek, K. et al. Proteins (2015) 83:1262-1272. DOI 10.1002/prot.24816 · PubMed

Other PDB entries of the same protein (UniProt Q07817 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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