3DAC

Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain

PDB DOI: https://doi.org/10.2210/pdb3DAC/pdb

Classification: CELL CYCLE
Organism(s): Danio rerio, Homo sapiens
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2008-05-29 Released: 2008-09-02
Deposition Author(s): Popowicz, G.M., Czarna, A., Holak, T.A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.243
R-Value Work: 0.205
R-Value Observed: 0.207

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

This is version 1.5 of the entry. See complete history.

Literature

Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain.

Popowicz, G.M., Czarna, A., Holak, T.A.

(2008) Cell Cycle 7: 2441-2443

PubMed: 18677113 Search on PubMed
DOI: https://doi.org/10.4161/cc.6365
Primary Citation of Related Structures:
3DAB, 3DAC

PubMed Abstract:
The Mdmx oncoprotein has only recently emerged as a critical-independent to Mdm2-regulator of p53 activation. We have determined the crystal structure of the N-terminal domain of human Mdmx bound to a 15-residue transactivation domain peptide of human p53. The structure shows why antagonists of the Mdm2 binding to p53 are ineffective in the Mdmx-p53 interaction.

Macromolecule Content

Total Structure Weight: 34.35 kDa
Atom Count: 1,750
Modelled Residue Count: 195
Deposited Residue Count: 302
Unique protein chains: 2

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Mdm4 protein	A [auth M], C [auth A]	130	Danio rerio	Mutation(s): 2 Gene Names: mdm4, mdmx
UniProt
Find proteins for Q7ZUW7 (Danio rerio) Explore Q7ZUW7 Go to UniProtKB: Q7ZUW7
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q7ZUW7
Sequence Annotations Expand
Reference Sequence

Find similar proteins by: Sequence | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
Cellular tumor antigen p53	B [auth P], D [auth B]	21	N/A	Mutation(s): 0
UniProt & NIH Common Fund Data Resources
Find proteins for P04637 (Homo sapiens) Explore P04637 Go to UniProtKB: P04637
PHAROS: P04637 GTEx: ENSG00000141510
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P04637
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.243
R-Value Work: 0.205
R-Value Observed: 0.207
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 66.43	α = 90
b = 30.81	β = 107.43
c = 70.09	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
MAR345	data collection
XDS	data reduction
XSCALE	data scaling
MOLREP	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2008-09-02

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2008-09-02
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2017-10-25
Changes: Refinement description
Version 1.3: 2019-11-06
Changes: Data collection, Database references
Version 1.4: 2021-11-10
Changes: Database references
Version 1.5: 2023-11-01
Changes: Data collection, Refinement description

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.