3VEK: Both Zn Fingers of GATA1

Both Zn Fingers of GATA1 Bound to Palindromic DNA Recognition Site, P1 Crystal Form. Determined by X-ray diffraction at 2.63 Å resolution. Released 16 Jan 2013.

Method
X-ray diffraction
Resolution
2.63 Å
Organisms
synthetic construct, Mus musculus
Chains
6
Atoms
3,154
Mol. weight
52.46 kDa
Ligands
ZN
Released
16 Jan 2013

Explore 3VEK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3VEK contains 12 α-helices and 8 β-strands across 2 chains. 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.

Chains C and F: 6 helices, 4 β-strands

ElementResiduesLengthSheet
β-strand216-21721
β-strand223-22421
α-helix226-23510
α-helix238-2403
β-strand270-27122
β-strand277-27822
α-helix280-28910
α-helix292-2943
α-helix295-2973
α-helix298-2992

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA (5'-d(*tp*tp*gp*tp*cp*tp*tp*ap*tp*cp*ap*gp*ap*tp*gp*gp*ap*cp*tp*c)-3')A, DDNA20synthetic construct
DNA (5'-d(*ap*ap*gp*ap*gp*tp*cp*cp*ap*tp*cp*tp*gp*ap*tp*ap*ap*gp*ap*c)-3')B, EDNA20synthetic construct
Erythroid transcription factorC, Fprotein119Mus musculusP17679 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>3VEK_1 DNA (5'-D(*TP*TP*GP*TP*CP*TP*TP*AP*TP*CP*AP*GP*AP*TP*GP*GP*AP*CP*TP*C)-3') (chains A, D)
TTGTCTTATCAGATGGACTC
Sequence of entity 2 (B, E), FASTA
>3VEK_2 DNA (5'-D(*AP*AP*GP*AP*GP*TP*CP*CP*AP*TP*CP*TP*GP*AP*TP*AP*AP*GP*AP*C)-3') (chains B, E)
AAGAGTCCATCTGATAAGAC
Sequence of entity 3 (C, F), FASTA
>3VEK_3 Erythroid transcription factor (chains C, F)
EARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRMIVSKRAGTQCT
NCQTTTTTLWRRNASGDPVCNACGLYFKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRG

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn14

Primary citation

GATA1 directly mediates interactions with closely spaced pseudopalindromic but not distantly spaced double GATA sites on DNA. Wilkinson-White, L., Lester, K.L., Ripin, N. et al. Protein Sci (2015) 24:1649-1659. DOI 10.1002/pro.2760 · PubMed

Other PDB entries of the same protein (UniProt P17679 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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