4MZI: Human mutant p53

Crystal structure of a human mutant p53. Determined by X-ray diffraction at 1.25 Å resolution. Released 15 Jan 2014.

Method
X-ray diffraction
Resolution
1.25 Å
Organism
Homo sapiens
Chains
1
Atoms
1,733
Mol. weight
22.6 kDa
Ligands
ZN
Released
15 Jan 2014

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

Secondary structure: helices and β-sheets

4MZI contains 8 α-helices and 12 β-strands across 1 chain. 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: 8 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix97-993
β-strand10311
β-strand110-11232
α-helix119-1202
β-strand124-12741
β-strand132-13541
β-strand141-14662
α-helix150-1523
β-strand156-16381
α-helix166-1683
α-helix172-1732
α-helix177-1804
β-strand195-19842
β-strand204-20741
β-strand214-21961
α-helix222-2243
β-strand230-23672
β-strand251-25881
β-strand264-274111
α-helix278-28710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cellular tumor antigen p53Aprotein200Homo sapiensP04637 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4MZI_1 Cellular tumor antigen p53 (chains A)
MSSSVPSQKTYQGSYGFRLGFLHSGTAKFGTCTYSPALNKMFVQLAKTVPVQLYVDSTPP
PGTRVRAMAIYKQSQHMTEVVRRCPHHERSSDSDGLAPPQHLIRVEGNLRAEYLDDPNTF
RHSVVVPYEPPEVGSDYTTIYFKFMCNSSCMGGMNRRPILVIITLEDSSGNLLGRDSFEV
RVCACPGRDRRTEEENLRKK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

Reversal of the DNA-Binding-Induced Loop L1 Conformational Switch in an Engineered Human p53 Protein. Emamzadah, S., Tropia, L., Vincenti, I. et al. J Mol Biol (2014) 426:936-944. DOI 10.1016/j.jmb.2013.12.020 · PubMed

Other PDB entries of the same protein (UniProt P04637 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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