3U15: Protein Mdm4

Structure of hDMX with Dimer Inducing Indolyl Hydantoin RO-2443. Determined by X-ray diffraction at 1.8 Å resolution. Released 27 Jun 2012.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,896
Mol. weight: 46.55 kDa
Ligands: 03M
Released: 27 Jun 2012

Explore 3U15 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3U15 contains 16 α-helices and 31 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: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27	1	1
β-strand	29	1	2
α-helix	31-38	8
β-strand	47	1	1
α-helix	49-62	14
β-strand	66	1	3
β-strand	73-75	3	3
α-helix	80-85	6
β-strand	89-91	3	3
α-helix	96-105	10
β-strand	106	1	2

Chain B: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	27	1	4
β-strand	29	1	5
α-helix	31-39	9
β-strand	47	1	4
α-helix	49-63	15
β-strand	66	1	6
β-strand	73	1	7
β-strand	74	1	6
α-helix	80-85	6
β-strand	91	1	7
β-strand	94	1	7
α-helix	96-105	10
β-strand	106	1	5

Chain C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27	1	8
β-strand	29	1	9
α-helix	31-40	10
β-strand	47	1	8
α-helix	49-62	14
β-strand	66-67	2	10
β-strand	70-75	6	10
α-helix	80-85	6
β-strand	89-91	3	10
α-helix	96-102	7
β-strand	106	1	9

Chain D: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	27	1	11
α-helix	31-39	9
β-strand	47	1	11
α-helix	49-62	14
β-strand	66	1	12
β-strand	73-75	3	12
β-strand	77	1	13
β-strand	79	1	13
α-helix	82-85	4
β-strand	89-91	3	12
β-strand	94	1	12
α-helix	96-104	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein Mdm4	A, B, C, D	protein	100	Homo sapiens	O15151 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3U15_1 Protein Mdm4 (chains A, B, C, D)
GPDSASRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQ
HMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLAT

Ligands and cofactors

ID	Name	Formula	Copies
03M	(5Z)-5-[(6-chloro-7-methyl-1H-indol-3-yl)methylidene]-3-(3,4-difluorobenzyl)imi…	C20 H14 Cl F2 N3 O2	4

Water and common crystallization additives (SO4) are not listed.

Primary citation

Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization. Graves, B., Thompson, T., Xia, M. et al. Proc Natl Acad Sci U S A (2012) 109:11788-11793. DOI 10.1073/pnas.1203789109 · PubMed

Other PDB entries of the same protein (UniProt O15151 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6Q9Y 1.2 Å, HDMX (14-111; C17S) COMPLEXED WITH COMPOUND 16 AT 1.20A; Structural states of Hdm2 and…
3FEA 1.33 Å, Crystal Structure of HdmX bound to the p53-peptidomimetic…
3FE7 1.35 Å, Crystal Structure of HdmX bound to the p53-peptidomimetic…
3FDO 1.4 Å, Structure of human MDMX in complex with high affinity peptide
3LBJ 1.5 Å, Structure of human MDMX protein in complex with a small molecule inhibitor
4RXZ 1.55 Å, Crystal Structure of MDMX phosporylated Tyr99 in complex with a 12-mer peptide
6Q9W 1.55 Å, X-ray structure of compound 15 bound to HdmX: Structural states of Hdm2 and HdmX: X-ray…
3EQY 1.63 Å, Crystal structure of human MDMX in complex with a 12-mer peptide inhibitor
7C3Y 1.63 Å, Crystal structure of the N-terminal domain of human MdmX protein in complex with Nutlin3a
7C44 1.65 Å, Crystal structure of the p53-binding domain of human MdmX protein in complex with Nutlin3a
8HDG 1.73 Å, Small peptide enhances the binding of nutline-3a to MdmX
3JZP 1.74 Å, Human MDMX liganded with a 12mer peptide inhibitor (pDI6W)

Browse structure collections

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