8IQL: Apoptosis regulator Bcl-2

Name: PDB 8IQL: Structural basis of the specificity and interaction mechanism of Bmf binding to pro-survival proteins
Published: 2023-08-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: apoptosis

Structural basis of the specificity and interaction mechanism of Bmf binding to pro-survival proteins. Determined by X-ray diffraction at 2.96 Å resolution. Released 23 Aug 2023.

Method: X-ray diffraction
Resolution: 2.96 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,557
Mol. weight: 44.72 kDa
Released: 23 Aug 2023

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

Secondary structure: helices and β-sheets

8IQL contains 20 α-helices and 0 β-strands across 4 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

Element	Residues	Length
α-helix	12-24	13
α-helix	91-107	17
α-helix	110-117	8
α-helix	126-137	12
α-helix	144-163	20
α-helix	169-180	12
α-helix	181-185	5
α-helix	186-190	5
α-helix	194-201	8

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	33-45	13

Chain C: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	11-24	14
α-helix	91-107	17
α-helix	109-116	8
α-helix	126-137	12
α-helix	144-162	19
α-helix	167-180	14
α-helix	181-185	5
α-helix	186-191	6
α-helix	194-201	8

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	33-46	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptosis regulator Bcl-2	A, C	protein	166	Homo sapiens	P10415 (AlphaFold model), Q07817 (AlphaFold model)
Bcl-2-modifying factor	B, D	protein	25	Homo sapiens	Q96LC9 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>8IQL_1 Apoptosis regulator Bcl-2 (chains A, C)
MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDDVEENRTEAPEGTESEVVHLTLRQAG
DDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVES
VNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMR

Sequence of entity 2 (B, D), FASTA

>8IQL_2 Bcl-2-modifying factor (chains B, D)
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 P10415 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8HTS 1.25 Å, Crystal structure of Bcl2 in complex with S-10r
6GL8 1.4 Å, Crystal structure of Bcl-2 in complex with the novel orally active inhibitor S55746
6QGG 1.5 Å, Structure of human Bcl-2 in complex with analogue of ABT-737
9IGG 1.5 Å, Structure of human Bcl-xL in complex with small molecule inhibitor
8HTR 1.6 Å, Crystal structure of Bcl2 in complex with S-9c
6O0K 1.62 Å, crystal structure of BCL-2 with venetoclax
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
9O16 1.73 Å, Crystal Structure of human BCL-2 (R129L) mutant in complex with a stapled BAD BH3…
6O0M 1.75 Å, crystal structure of BCL-2 F104L mutation with venetoclax
5VAU 1.75 Å, Bcl-2 complex with Beclin 1 BH3 domain
8VWX 1.77 Å, Human Bcl-2 (G101V Mutant)/Bcl-xL Chimera Fused to Maltose-Binding Protein

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