1srk Summary

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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)search. 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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Zinc finger protein ZFPM1 O35615 (328-360) (FOG1_MOUSE)search Mus musculussearch < 90% 35 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O35615 (328 - 360) Zinc finger protein ZFPM1 Mus musculus

Chain Structural classification (SCOP) Sequence family (Pfam)
A Classic zinc finger, C2H2search Zinc-finger double domainsearch

Chain ID Molecular function (GO)
A (O35615) nucleic acid bindingsearch metal ion bindingsearch

Chain InterPro annotation
A Zinc finger, C2H2search Zinc finger C2H2-type/integrase DNA-binding domainsearch Zinc finger, C2H2-likesearch