4HNJ: Bcl-2-like protein 1

Crystallographic structure of BCL-xL domain-swapped dimer in complex with PUMA BH3 peptide at 2.9A resolution. Determined by X-ray diffraction at 2.9 Å resolution. Released 23 Jan 2013.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Homo sapiens
Chains
3
Atoms
2,334
Mol. weight
50.39 kDa
Released
23 Jan 2013

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

Secondary structure: helices and β-sheets

4HNJ contains 19 α-helices and 0 β-strands across 3 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: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix0-1920
α-helix83-10119
α-helix102-1043
α-helix108-1125
α-helix116-1183
α-helix119-13012
α-helix137-17337
α-helix174-1785
α-helix179-1846
α-helix187-1948
Chain B: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1-1919
α-helix23-275
α-helix83-10018
α-helix123-1308
α-helix137-17337
α-helix174-1785
α-helix179-1846
α-helix187-1948
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix304-32219

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bcl-2-like protein 1A, Bprotein212Homo sapiensQ07817 (AlphaFold model)
Bcl-2-binding component 3Cprotein25Homo sapiensQ9BXH1 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4HNJ_1 Bcl-2-like protein 1 (chains A, B)
GSHMSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSW
HLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPG
TAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDH
LEPWIQENGGWDTFVELYGNNAAAESRKGQER
Sequence of entity 2 (C), FASTA
>4HNJ_2 Bcl-2-binding component 3 (chains C)
EEQWAREIGAQLRRMADDLNAQYER

Primary citation

PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis. Follis, A.V., Chipuk, J.E., Fisher, J.C. et al. Nat Chem Biol (2013) 9:163-168. DOI 10.1038/nchembio.1166 · PubMed

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

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