5C3F: Mcl-1

Crystal structure of Mcl-1 bound to BID-MM. Determined by X-ray diffraction at 1.43 Å resolution. Released 20 Apr 2016.

Method: X-ray diffraction
Resolution: 1.43 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,611
Mol. weight: 20.58 kDa
Released: 20 Apr 2016

Explore 5C3F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5C3F 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	173-191	19
α-helix	198-199	2
α-helix	203-223	21
α-helix	225-235	11
α-helix	240-242	3
α-helix	244-253	10
α-helix	254-256	3
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	81-100	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Induced myeloid leukemia cell differentiation protein Mcl-1	A	protein	156	Homo sapiens	Q07820 (AlphaFold model)
Bid-mm	B	protein	24	Homo sapiens	P55957 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5C3F_1 Induced myeloid leukemia cell differentiation protein Mcl-1 (chains A)
SELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGM
LRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLA
ESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGG

Sequence of entity 2 (B), FASTA

>5C3F_2 BID-MM (chains B)
XEDIIRNIARHLALVGDLLDRSIW

Primary citation

Hydrocarbon constrained peptides - understanding preorganisation and binding affinity. Miles, J.A., Yeo, D.J., Rowell, P. et al. Chem Sci (2016) 7:3694-3702. DOI 10.1039/c5sc04048e · PubMed

Other PDB entries of the same protein (UniProt Q07820 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8VJP 1.13 Å, Histidine-covalent stapled alpha-helical peptide (155H1) targeting hMcl-1
9PQ7 1.24 Å, MBP-Mcl1 in complex with ligand 21b
9PQ5 1.28 Å, MBP-Mcl1 in complex with ligand 8
6UDV 1.35 Å, X-ray co-crystal structure of compound 3 bound to human Mcl-1
9UGP 1.39 Å, Crystal structure of MCL-1 in complex with HRK BH3
8G3S 1.4 Å, MBP-Mcl1 in complex with ligand 11
5W89 1.42 Å, Crystal structure of human Mcl-1 in complex with modified Bim BH3 peptide SAH-MS1-18
8G3X 1.46 Å, MBP-Mcl1 in complex with ligand 32
8H7B 1.46 Å, The crystal structure of human mcl1 kinase domain in complex with MCL1-M-EBA
8SVY 1.47 Å, MBP-Mcl1 in complex with ligand 10
6OQD 1.48 Å, Crystal structure of Mcl1 with inhibitor 8
5FC4 1.5 Å, Mcl-1 complexed with small molecule inhibitor

Browse structure collections

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