4BPJ: Mcl-1

Mcl-1 bound to alpha beta Puma BH3 peptide 3. Determined by X-ray diffraction at 1.6 Å resolution. Released 9 Apr 2014.

Method: X-ray diffraction
Resolution: 1.6 Å
Organisms: MUS MUSCULUS, HOMO SAPIENS
Chains: 2
Atoms: 1,558
Mol. weight: 20.8 kDa
Ligands: ZN
Released: 9 Apr 2014

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

Secondary structure: helices and β-sheets

4BPJ contains 8 α-helices and 0 β-strands across 2 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: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	173-191	19
α-helix	204-223	20
α-helix	225-238	14
α-helix	245-254	10
α-helix	261-281	21
α-helix	288-308	21
α-helix	311-318	8

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	90-104	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fusion protein consisting of induced myeloid leukemia cell differentiation protein mcl-1 homolog	A	protein	162	MUS MUSCULUS, HOMO SAPIENS	P97287 (AlphaFold model), Q07820 (AlphaFold model)
Alpha beta BH3-peptide	D	protein	19	HOMO SAPIENS	Q9BXH1 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4BPJ_1 FUSION PROTEIN CONSISTING OF INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL-1 HOMOLOG (chains A)
GPLGSEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHE
TAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQES
CIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGG

Sequence of entity 2 (D), FASTA

>4BPJ_2 ALPHA BETA BH3-PEPTIDE (chains D)
AIAAXLRRMADDLNAQYEX

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	5

Water and common crystallization additives (CL) are not listed.

Primary citation

Structure-Guided Rational Design of Alpha/Beta-Peptide Foldamers with High Affinity for Bcl-2 Family Prosurvival Proteins. Smith, B.J., Lee, E.F., Checco, J.W. et al. Chembiochem (2013) 14:1564. DOI 10.1002/CBIC.201300351 · PubMed

Other PDB entries of the same protein (UniProt P97287 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2NL9 1.55 Å, Crystal structure of the Mcl-1:Bim BH3 complex
5VX2 1.85 Å, Mcl-1 in complex with Bim-h3Pc-RT
4BPI 1.98 Å, Mcl-1 bound to alpha beta Puma BH3 peptide 2
4G35 2.0 Å, Mcl-1 in complex with a biphenyl cross-linked Noxa peptide.
3D7V 2.03 Å, Crystal structure of Mcl-1 in complex with an Mcl-1 selective BH3 ligand
5KU9 2.2 Å, Crystal structure of MCL1 with compound 1
5MES 2.24 Å, MCL1 FAB complex in complex with compound 29
3IO9 2.4 Å, BimL12Y in complex with Mcl-1
6DM8 2.7 Å, Understanding the Species Selectivity of Myeloid cell leukemia-1 (Mcl-1) inhibitors
2NLA 2.8 Å, Crystal structure of the Mcl-1:mNoxaB BH3 complex
5MEV 2.94 Å, MCL1 FAB complex in complex with compound 21
1WSX Solution structure of MCL-1

Browse structure collections

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