3IO9: BimL12Y

BimL12Y in complex with Mcl-1. Determined by X-ray diffraction at 2.4 Å resolution. Released 1 Sept 2009.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Homo sapiens, Mus musculus
Chains: 2
Atoms: 1,423
Mol. weight: 21.81 kDa
Ligands: ZN
Released: 1 Sept 2009

Explore 3IO9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3IO9 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	204-221	18
α-helix	225-235	11
α-helix	244-254	11
α-helix	261-280	20
α-helix	288-308	21
α-helix	312-318	7

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	54-74	21

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>3IO9_1 Induced myeloid leukemia cell differentiation protein Mcl-1 (chains A)
GPLGSEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHE
TAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQES
CIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGG

Sequence of entity 2 (B), FASTA

>3IO9_2 Bcl-2-like protein 11 (chains B)
DMRPEIWIAQEYRRIGDEFNAYYARR

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Primary citation

Conformational changes in Bcl-2 pro-survival proteins determine their capacity to bind ligands. Lee, E.F., Czabotar, P.E., Yang, H. et al. J Biol Chem (2009) 284:30508-30517. DOI 10.1074/jbc.M109.040725 · 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
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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