› 1srk

Solution NMR

Solution structure of the third zinc finger domain of FOG-1

Released:
DOI: 10.2210/pdb1srk/pdb
PDB entry 1srk coloured by chain, ensemble of 20 models, front view.
PDB entry 1srk coloured by chain, ensemble of 20 models, side view.
PDB entry 1srk coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
A classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3.
Simpson RJ, Yi Lee SH, Bartle N, Sum EY, Visvader JE, Matthews JM, Mackay JP, Crossley M
J Biol Chem 279 39789-97 (2004)
PMID: 15234987

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128696 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Zinc finger protein ZFPM1 Chain: A
Molecule details ›
Chain: A
Length: 35 amino acids
Theoretical weight: 3.81 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O35615 (Residues: 328-360; Coverage: 3%)
Gene names: Fog, Fog1, Zfpm1

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, molecular dynamics, torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Keep your fingers off my DNA: protein-protein interactions mediated by C2H2 zinc finger domains.
Brayer et al. (2008)
4 more

2 mentions without citation

Structural basis for interaction between CLAMP and MSL2 proteins involved in the specific recruitment of the dosage compensation complex in Drosophila.
Tikhonova et al. (2022)
1 more