› 3vd6

X-ray diffraction
1.98Å resolution

Both Zn Fingers of GATA1 Bound to Palindromic DNA Recognition Site, P21 Crystal Form

Released:
DOI: 10.2210/pdb3vd6/pdb
PDB entry 3vd6 coloured by chain, front view.
PDB entry 3vd6 coloured by chain, side view.
PDB entry 3vd6 coloured by chain, top view.
Source organisms:
Primary publication:
GATA1 directly mediates interactions with closely spaced pseudopalindromic but not distantly spaced double GATA sites on DNA.
Wilkinson-White L, Lester KL, Ripin N, Jacques DA, Mitchell Guss J, Matthews JM
Protein Sci 24 1649-59 (2015)
PMID: 26234528

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-216169 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Erythroid transcription factor Chain: C
Molecule details ›
Chain: C
Length: 119 amino acids
Theoretical weight: 13.51 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P17679 (Residues: 200-318; Coverage: 29%)
Gene names: Gata1, Gf-1
Sequence domains: GATA zinc finger
Structure domains: Erythroid Transcription Factor GATA-1, subunit A
DNA (5'-D(*TP*TP*GP*TP*CP*TP*TP*AP*TP*CP*AP*GP*AP*TP*GP*GP*AP*CP*TP*C)-3') Chain: A
Molecule details ›
Chain: A
Length: 20 nucleotides
Theoretical weight: 6.11 KDa
Source organism: synthetic construct
Expression system: Not provided
DNA (5'-D(*AP*AP*GP*AP*GP*TP*CP*CP*AP*TP*CP*TP*GP*AP*TP*AP*AP*GP*AP*C)-3') Chain: B
Molecule details ›
Chain: B
Length: 20 nucleotides
Theoretical weight: 6.15 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 54.331Å b: 37.401Å c: 65.484Å
α: 90° β: 98.51° γ: 90°
R-values:
R R work R free
0.22 0.218 0.247
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

GATA factor mutations in hematologic disease.
Crispino et al. (2017)
2 more

5 mentions without citation

Targeting GATA4 for cardiac repair.
Välimäki et al. (2020)
4 more