Solution structure of the third zinc finger domain of FOG-1
The structure was published by Simpson, R.J.Y., Lee, S.H.Y., Bartle, N., et al., Matthews, J.M., Mackay, J.P., and Crossley, M., in 2004 in a paper entitled "A Classic Zinc Finger from Friend of GATA Mediates an Interaction with the Coiled-coil of Transforming Acidic Coiled-coil 3." (abstract).
The structure was determined using NMR spectroscopy and deposited in 2004.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Zinc finger protein ZFPM1. This molecule has the UniProt identifier O35615 (FOG1_MOUSE). The sample contained 35 residues which is < 90% of the natural sequence. Out of 35 residues 35 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: