2P1L: Bcl-XL:Beclin 1 complex

Structure of the Bcl-XL:Beclin 1 complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Mar 2007.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 8
Atoms: 5,300
Mol. weight: 83.55 kDa
Released: 13 Mar 2007

Explore 2P1L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2P1L contains 36 α-helices and 8 β-strands across 8 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: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
α-helix	26-102	21
β-strand	110	1	1
β-strand	112	1	1
α-helix	116-130	15
α-helix	137-156	20
α-helix	162-173	12
α-helix	174-178	5
α-helix	179-184	6
α-helix	187-195	9

Chains B, D, F and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	107-125	19

Chain C: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
α-helix	26-102	21
β-strand	110	1	2
β-strand	112	1	2
α-helix	119-131	13
α-helix	137-156	20
α-helix	162-173	12
α-helix	174-178	5
α-helix	179-184	6
α-helix	187-195	9

Chain E: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	5-18	14
α-helix	26-102	21
β-strand	110	1	3
β-strand	112	1	3
α-helix	119-130	12
α-helix	137-156	20
α-helix	161-173	13
α-helix	174-178	5
α-helix	179-184	6
α-helix	187-195	9

Chain G: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
α-helix	26-102	21
β-strand	110	1	4
β-strand	112	1	4
α-helix	119-130	12
α-helix	137-156	20
α-helix	161-173	13
α-helix	174-178	5
α-helix	179-184	6
α-helix	187-195	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptosis regulator Bcl-X	A, C, E, G	protein	153	Homo sapiens	Q07817 (AlphaFold model)
Beclin 1	B, D, F, H	protein	31	Homo sapiens	Q14457 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>2P1L_1 Apoptosis regulator Bcl-X (chains A, C, E, G)
MSQSNRELVVDFLSYKLSQKGYSWSQMAAVKQALREAGDEFELRYRRAFSDLTSQLHITP
GTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLND
HLEPWIQENGGWDTFVELYGNNAAAESRKGQER

Sequence of entity 2 (B, D, F, H), FASTA

>2P1L_2 Beclin 1 (chains B, D, F, H)
GSGTMENLSRRLKVTGDLFDIMSGQTDVDHP

Primary citation

Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. Oberstein, A., Jeffrey, P.D., Shi, Y. J Biol Chem (2007) 282:13123-13132. DOI 10.1074/jbc.M700492200 · PubMed

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

7JGW 1.3 Å, Crystal structure of BCL-XL in complex with COMPOUND 1620116, CRYSTAL FORM 1
3SP7 1.4 Å, Crystal Structure of Bcl-xL bound to BM903
7YAA 1.4 Å, Crystal structure analysis of cp3 bound BCLxl
7LH7 1.41 Å, Crystal structure of BCL-XL in complex with a benzothiazole-based inhibitor
9IGG 1.5 Å, Structure of human Bcl-xL in complex with small molecule inhibitor
4QVF 1.53 Å, Crystal structure of Bcl-xL in complex with BIM BH3 domain
4A1U 1.54 Å, Crystal structure of alpha-beta-foldamer 2c in complex with Bcl-xL
6VWC 1.6 Å, Crystal structure of Bcl-xL in complex with tetrahydroisoquinoline-pyridine based…
6O0K 1.62 Å, crystal structure of BCL-2 with venetoclax
3SPF 1.7 Å, Crystal Structure of Bcl-xL bound to BM501
9I9E 1.7 Å, Structure of human Bcl-xL in complex with small molecule inhibitor
9O14 1.73 Å, Crystal Structure of BCL-2 in complex with a stapled BAD BH3 peptide BAD SAHB 4.2

Browse structure collections

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