2ROC: Mcl-1

Solution structure of Mcl-1 Complexed with Puma. Determined by solution NMR. Released 8 Jul 2008.

Method: Solution NMR
Organism: Mus musculus
Chains: 2
Atoms: 1,521
Mol. weight: 21.59 kDa
Released: 8 Jul 2008

Explore 2ROC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ROC contains 12 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	149-151	3
α-helix	154-172	19
α-helix	180-182	3
α-helix	185-204	20
α-helix	206-215	10
α-helix	222-234	13
α-helix	235-237	3
α-helix	242-261	20
α-helix	265-282	18
α-helix	284-289	6
α-helix	293-300	8

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	132-153	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Induced myeloid leukemia cell differentiation protein Mcl-1 homolog	A	protein	162	Mus musculus	P97287 (AlphaFold model)
Bcl-2-binding component 3	B	protein	27	Mus musculus	Q99ML1 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2ROC_1 Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (chains A)
GPLGSEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHE
TAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQES
FIEPLAETITDVLVRTKRDWLVKQRGWDGFVEFFHVQDLEGG

Sequence of entity 2 (B), FASTA

>2ROC_2 Bcl-2-binding component 3 (chains B)
EEEWAREIGAQLRRIADDLNAQYERRM

Primary citation

Structure of the BH3 Domains from the p53-Inducible BH3-Only Proteins Noxa and Puma in Complex with Mcl-1. Day, C.L., Smits, C., Fan, F.C. et al. J Mol Biol (2008) 380:958-971. DOI 10.1016/j.jmb.2008.05.071 · 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
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

Browse structure collections

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