4HW4: PDB entry 4HW4

Discovery of potent Mcl-1 inhibitors using fragment-based methods and structure-based design. Determined by X-ray diffraction at 1.53 Å resolution. Released 9 Jan 2013.

Method: X-ray diffraction
Resolution: 1.53 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,041
Mol. weight: 39.4 kDa
Released: 9 Jan 2013

Explore 4HW4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4HW4 contains 26 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: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	173-191	19
α-helix	203-212	10
α-helix	213-217	5
α-helix	218-223	6
α-helix	225-235	11
α-helix	240-253	14
α-helix	254-256	3
α-helix	261-280	20
α-helix	284-286	3
α-helix	287-296	10
α-helix	297-301	5
α-helix	303-308	6
α-helix	311-319	9
α-helix	320-322	3

Chain B: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	173-190	18
α-helix	204-223	20
α-helix	225-235	11
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	311-318	8

Chains C and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-15	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Induced myeloid leukemia cell differentiation protein Mcl-1	A, B	protein	157	Homo sapiens	Q07820 (AlphaFold model)
Mcl-1 BH3 peptide	C, D	protein	18

Sequence of entity 1 (A, B), FASTA

>4HW4_1 Induced myeloid leukemia cell differentiation protein Mcl-1 (chains A, B)
GDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQG
MLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPL
AESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGG

Sequence of entity 2 (C, D), FASTA

>4HW4_2 Mcl-1 BH3 peptide (chains C, D)
XALETLRRVGDGVQRNHX

Primary citation

Discovery of potent myeloid cell leukemia 1 (Mcl-1) inhibitors using fragment-based methods and structure-based design. Friberg, A., Vigil, D., Zhao, B. et al. J Med Chem (2013) 56:15-30. DOI 10.1021/jm301448p · 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

Browse structure collections

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