3DAB: Human Mdmx protein

Name: PDB 3DAB: Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain
Published: 2008-09-02
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: cell cycle

Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain. Determined by X-ray diffraction at 1.9 Å resolution. Released 2 Sept 2008.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 8
Atoms: 3,580
Mol. weight: 48.33 kDa
Released: 2 Sept 2008

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

Secondary structure: helices and β-sheets

3DAB contains 20 α-helices and 24 β-strands across 8 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.

Chains A and G: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	27-29	3	1
α-helix	31-39	9
β-strand	47	1	1
α-helix	49-62	14
β-strand	66	1	2
β-strand	73-75	3	2
α-helix	80-85	6
β-strand	89-91	3	2
α-helix	96-105	10
β-strand	106-108	3	1

Chains B, F and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	19-24	6

Chain C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	27	1	3
β-strand	29	1	4
α-helix	31-39	9
β-strand	47	1	3
α-helix	49-62	14
β-strand	66	1	5
β-strand	73-75	3	5
α-helix	80-85	6
β-strand	89-91	3	5
α-helix	96-105	10
β-strand	106	1	4

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	19-23	5

Chain E: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	27	1	6
α-helix	31-39	9
β-strand	47	1	6
α-helix	49-62	14
β-strand	66	1	7
β-strand	73-75	3	7
α-helix	80-85	6
β-strand	89-91	3	7
α-helix	96-105	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mdm4 protein	A, C, E, G	protein	90	Homo sapiens	O15151 (AlphaFold model)
Cellular tumor antigen p53	B, D, F, H	protein	15		P04637 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>3DAB_1 Mdm4 protein (chains A, C, E, G)
IQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLL
GELLGRQSFSVKDPSPLYDMLRKNLVTLAT

Sequence of entity 2 (B, D, F, H), FASTA

>3DAB_2 Cellular tumor antigen p53 (chains B, D, F, H)
SQETFSDLWKLLPEN

Primary citation

Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain. Popowicz, G.M., Czarna, A., Holak, T.A. Cell Cycle (2008) 7:2441-2443. DOI 10.4161/cc.6365 · 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)

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