5VX2: Mcl-1

Mcl-1 in complex with Bim-h3Pc-RT. Determined by X-ray diffraction at 1.85 Å resolution. Released 15 Nov 2017.

Method: X-ray diffraction
Resolution: 1.85 Å
Organisms: Mus musculus, Homo sapiens
Chains: 4
Atoms: 3,119
Mol. weight: 43.12 kDa
Released: 15 Nov 2017

Explore 5VX2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5VX2 contains 22 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	173-191	19
α-helix	197-199	3
α-helix	205-235	31
α-helix	240-242	3
α-helix	243-253	11
α-helix	254-256	3
α-helix	261-280	20
α-helix	284-286	3
α-helix	287-308	22
α-helix	311-318	8

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	54-74	21

Chain C: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	173-191	19
α-helix	197-199	3
α-helix	203-235	33
α-helix	241-243	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	311-318	8

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	52-74	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Induced myeloid leukemia cell differentiation protein Mcl-1 homolog,Induced myeloid leukemia cell…	A, C	protein	162	Mus musculus, Homo sapiens	P97287 (AlphaFold model), Q07820 (AlphaFold model)
Bcl-2-like protein 11	B, D	protein	26	Homo sapiens	O43521 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>5VX2_1 Induced myeloid leukemia cell differentiation protein Mcl-1 homolog,Induced myeloid leukemia cell differentiation protein Mcl-1 chimera (chains A, C)
GPLGSEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHE
TAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQES
CIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGG

Sequence of entity 2 (B, D), FASTA

>5VX2_2 Bcl-2-like protein 11 (chains B, D)
DMRPEIRIAQELRRXGDEFNATYARR

Primary citation

Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design. Brouwer, J.M., Lan, P., Cowan, A.D. et al. Mol Cell (2017) 68:659-672.e9. DOI 10.1016/j.molcel.2017.11.001 · 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
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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