› 4kvp

X-ray diffraction
1.5Å resolution

Human p53 Core Domain Mutant V157F

Released:
DOI: 10.2210/pdb4kvp/pdb
PDB entry 4kvp coloured by chain, front view.
PDB entry 4kvp coloured by chain, side view.
PDB entry 4kvp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of oncogenic, suppressor and rescued p53 core-domain variants: mechanisms of mutant p53 rescue.
Wallentine BD, Wang Y, Tretyachenko-Ladokhina V, Tan M, Senear DF, Luecke H
Acta Crystallogr D Biol Crystallogr 69 2146-56 (2013)
PMID: 24100332

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular tumor antigen p53 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 220 amino acids
Theoretical weight: 24.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04637 (Residues: 94-312; Coverage: 56%)
Gene names: P53, TP53
Sequence domains: P53 DNA-binding domain
Structure domains: Immunoglobulin-like

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 68.656Å b: 70.279Å c: 83.559Å
α: 90° β: 90.06° γ: 90°
R-values:
R R work R free
0.176 0.174 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches.
Joerger et al. (2016)
1 more

6 mentions without citation

Structural and Drug Targeting Insights on Mutant p53.
Gomes et al. (2021)
5 more