2KBW: Human Mcl-1

Solution Structure of human Mcl-1 complexed with human Bid_BH3 peptide. Determined by solution NMR. Released 15 Dec 2009.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 1,524
Mol. weight: 22.45 kDa
Released: 15 Dec 2009

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

Secondary structure: helices and β-sheets

2KBW contains 10 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: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	173-191	19
α-helix	204-223	20
α-helix	225-235	11
α-helix	240-242	3
α-helix	243-254	12
α-helix	261-280	20
α-helix	287-301	15
α-helix	303-308	6
α-helix	313-319	7

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	79-99	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Induced myeloid leukemia cell differentiation protein Mcl-1	A	protein	164	Homo sapiens	Q07820 (AlphaFold model)
BH3-interacting domain death agonist	B	protein	35	Homo sapiens	P55957 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2KBW_1 Induced myeloid leukemia cell differentiation protein Mcl-1 (chains A)
TPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQR
NHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTIN
QESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEG

Sequence of entity 2 (B), FASTA

>2KBW_2 BH3-interacting domain death agonist (chains B)
GPLGSESQEDIIRNIARHLAQVGDSMDRSIPPGLV

Primary citation

Apoptotic regulation by MCL-1 through heterodimerization. Liu, Q., Moldoveanu, T., Sprules, T. et al. J Biol Chem (2010) 285:19615-19624. DOI 10.1074/jbc.M110.105452 · 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
5C3F 1.43 Å, Crystal structure of Mcl-1 bound to BID-MM
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

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