5VX3: Bcl-xL

Bcl-xL in complex with Bim-h3Pc-RT. Determined by X-ray diffraction at 1.95 Å resolution. Released 15 Nov 2017.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 8
Atoms: 5,862
Mol. weight: 85.45 kDa
Released: 15 Nov 2017

Explore 5VX3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5VX3 contains 44 α-helices and 0 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	2-19	18
α-helix	26-101	20
α-helix	103-105	3
α-helix	110-112	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 B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	86-103	18

Chain C: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	1-19	19
α-helix	26-100	19
α-helix	103-105	3
α-helix	110-112	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 D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	86-104	19

Chain E: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	1-19	19
α-helix	26-100	19
α-helix	102-105	4
α-helix	108-111	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

Chains F and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	86-105	20

Chain G: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	1-19	19
α-helix	26-100	19
α-helix	102-105	4
α-helix	108-112	5
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
Bcl-2-like protein 1	A, C, E, G	protein	158	Homo sapiens	Q07817 (AlphaFold model)
Bcl-2-like protein 11	B, D, F, H	protein	26	Homo sapiens	O43521 (AlphaFold model)

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

>5VX3_1 Bcl-2-like protein 1 (chains A, C, E, G)
GPLGSMSQSNRELVVDFLSYKLSQKGYSWSQMAAVKQALREAGDEFELRYRRAFSDLTSQ
LHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMA
TYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER

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

>5VX3_2 Bcl-2-like protein 11 (chains B, D, F, H)
DMRPEIRIAQELRRXGDEFNATYARR

Primary citation

Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design. Brouwer, J.M., Lan, P., Cowan, A.D. et al. Mol Cell (2017) 68:659-672.e9. DOI 10.1016/j.molcel.2017.11.001 · 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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