› 3us0

X-ray diffraction
2.5Å resolution

Structure of p63 DNA Binding Domain in Complex with a 22 Base Pair A/T Rich Response Element Containing a Two Base Pair "AT" Spacer Between Half Sites

Released:
DOI: 10.2210/pdb3us0/pdb
PDB entry 3us0 coloured by chain, front view.
PDB entry 3us0 coloured by chain, side view.
PDB entry 3us0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pliable DNA conformation of response elements bound to transcription factor p63.
Chen C, Gorlatova N, Herzberg O
J Biol Chem 287 7477-86 (2012)
PMID: 22247550

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-117003 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Tumor protein 63 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 203 amino acids
Theoretical weight: 22.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H3D4 (Residues: 166-362; Coverage: 29%)
Gene names: KET, P63, P73H, P73L, TP63, TP73L
Sequence domains: P53 DNA-binding domain
Structure domains: Immunoglobulin-like
5'-D(*AP*AP*AP*CP*AP*TP*GP*TP*TP*TP*AP*TP*AP*AP*AP*CP*AP*TP*GP*TP*TP*T)-3' Chains: E, F
Molecule details ›
Chains: E, F
Length: 22 nucleotides
Theoretical weight: 6.75 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P63
Unit cell:
a: 141.806Å b: 141.806Å c: 119.604Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.206 0.239
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

Roles of p53 Family Structure and Function in Non-Canonical Response Element Binding and Activation.
Cai et al. (2019)
1 more

7 mentions without citation

Disease-associated mutations disrupt functionally important regions of intrinsic protein disorder.
Vacic et al. (2012)
6 more