4G35: Mcl-1

Mcl-1 in complex with a biphenyl cross-linked Noxa peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 5 Dec 2012.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,255
Mol. weight: 21.16 kDa
Ligands: 4BP
Released: 5 Dec 2012

Explore 4G35 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4G35 contains 9 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: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	173-190	18
α-helix	207-223	17
α-helix	225-232	8
α-helix	246-253	8
α-helix	261-280	20
α-helix	284-286	3
α-helix	287-308	22
α-helix	311-319	9

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-19	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Induced myeloid leukemia cell differentiation protein Mcl-1 homolog	A	protein	165	Mus musculus	P97287 (AlphaFold model)
Noxa BH3 peptide (cysteine-mediated cross-linked)	B	protein	21

Sequence of entity 1 (A), FASTA

>4G35_1 Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (chains A)
GPLGSPEFEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQR
NHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVN
QESFIEPLAETITDVLVRTKRDWLVKQRGWDGFVEFFHVQDLEGG

Sequence of entity 2 (B), FASTA

>4G35_2 Noxa BH3 peptide (cysteine-mediated cross-linked) (chains B)
XAACLRRIGDCVNLRQKLLNX

Ligands and cofactors

ID	Name	Formula	Copies
4BP	4,4'-bis(bromomethyl)biphenyl	C14 H12 Br2	1

Primary citation

Rational design of proteolytically stable, cell-permeable peptide-based selective Mcl-1 inhibitors. Muppidi, A., Doi, K., Edwardraja, S. et al. J Am Chem Soc (2012) 134:14734-14737. DOI 10.1021/ja306864v · 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
4BPJ 1.6 Å, Mcl-1 bound to alpha beta Puma BH3 peptide 3
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
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

About this viewer

MolViewer shows 4G35 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.