2NLA: Mcl-1:mNoxaB BH3 complex

Crystal structure of the Mcl-1:mNoxaB BH3 complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 27 Mar 2007.

Method: X-ray diffraction
Resolution: 2.8 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 1,406
Mol. weight: 20.83 kDa
Released: 27 Mar 2007

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

Secondary structure: helices and β-sheets

2NLA contains 11 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	173-190	18
α-helix	203-223	21
α-helix	225-234	10
α-helix	240-253	14
α-helix	254-256	3
α-helix	261-280	20
α-helix	284-286	3
α-helix	287-301	15
α-helix	303-308	6
α-helix	312-318	7

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	77-90	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
FUSION PROTEIN CONSISTING OF Induced myeloid leukemia cell differentiation protein Mcl-1 homolog	A	protein	157	Mus musculus, Homo sapiens	P97287 (AlphaFold model), Q07820 (AlphaFold model)
Phorbol-12-myristate-13-acetate-induced protein 1	B	protein	26	Mus musculus	Q9JM54 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2NLA_1 FUSION PROTEIN CONSISTING OF Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (chains A)
EDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHETAFQG
MLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPL
AESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGG

Sequence of entity 2 (B), FASTA

>2NLA_2 Phorbol-12-myristate-13-acetate-induced protein 1 (chains B)
PADLKDECAQLRRIGDKVNLRQKLLN

Primary citation

Structural insights into the degradation of Mcl-1 induced by BH3 domains. Czabotar, P.E., Lee, E.F., van Delft, M.F. et al. Proc Natl Acad Sci U S A (2007) 104:6217-6222. DOI 10.1073/pnas.0701297104 · 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
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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