8IQK: Bcl-2-like protein 1

Structural basis of the specificity and interaction mechanism of Bmf binding to pro-survival proteins. Determined by X-ray diffraction at 2.88 Å resolution. Released 23 Aug 2023.

Method: X-ray diffraction
Resolution: 2.88 Å
Organism: Homo sapiens
Chains: 8
Atoms: 5,113
Mol. weight: 90.08 kDa
Released: 23 Aug 2023

Explore 8IQK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8IQK contains 45 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	5-19	15
α-helix	24-26	3
α-helix	86-104	19
α-helix	108-110	3
α-helix	119-130	12
α-helix	137-156	20
α-helix	161-173	13
α-helix	174-178	5
α-helix	179-182	4
α-helix	183-185	3
α-helix	189-194	6

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	130-142	13

Chain C: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	5-19	15
α-helix	24-26	3
α-helix	86-104	19
α-helix	108-110	3
α-helix	116-130	15
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 D, F and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	130-141	12

Chain E: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	5-19	15
α-helix	24-26	3
α-helix	85-104	20
α-helix	108-110	3
α-helix	119-130	12
α-helix	137-156	20
α-helix	161-173	13
α-helix	174-178	5
α-helix	179-183	5
α-helix	187-194	8

Chain G: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	5-19	15
α-helix	24-26	3
α-helix	86-104	19
α-helix	108-110	3
α-helix	116-130	15
α-helix	137-156	20
α-helix	161-173	13
α-helix	174-178	5
α-helix	179-183	5
α-helix	188-194	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bcl-2-like protein 1	A, C, E, G	protein	171	Homo sapiens	Q07817 (AlphaFold model)
Bcl-2-modifying factor	B, D, F, H	protein	25	Homo sapiens	Q96LC9 (AlphaFold model)

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

>8IQK_1 Bcl-2-like protein 1 (chains A, C, E, G)
MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMAAVKQALREAGDEFE
LRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKE
MQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER

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

>8IQK_2 Bcl-2-modifying factor (chains B, D, F, H)
HQAEVQIARKLQCIADQFHRLHVQQ

Primary citation

Structural basis of the specificity and interaction mechanism of Bmf binding to pro-survival Bcl-2 family proteins. Wang, H., Guo, M., Wei, H. et al. Comput Struct Biotechnol J (2023) 21:3760-3767. DOI 10.1016/j.csbj.2023.07.017 · 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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