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Zinc fingers as protein recognition motifs: structural basis for the gata-1/FRIEND of gata interaction

Analyse Zinc fingers as protein recognition motifs: structural basis for the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Y0J
Type
protein
Length
75 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Erythroid transcription factor; Zinc-finger protein ush
UniProt
P17679, Q9VPQ6
Ligands
ZN

Structure

solution nmr · 2 distinct chains · 19% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AErythroid transcription factorprotein3918% helix, 10% strandP17679
BZinc-finger protein ushprotein3619% helix, 6% strandQ9VPQ6

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 530 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 1Y0J · Zinc fingers as protein recognition motifs: structural basis for the GATA-1/Friend of… · the same entry in another collection · chain A against A, TM-score 1.00
  • P17679 · AlphaFold monomer V2.0 prediction for erythroid transcription factor (P17679) · a predicted model of the same protein · chain A against A, TM-score 0.70
  • Q9VPQ6 · AlphaFold monomer V2.0 prediction for zinc finger protein ush (Q9VPQ6) · a predicted model of the same protein · chain B against A, TM-score 0.54

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