1eh2 Summary

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STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES

The structure was published by de Beer, T., Carter, R.E., Lobel-Rice, K.E., Sorkin, A., and Overduin, M., in 1998 in a paper entitled "Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1998.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of EPS15. This molecule has the UniProt identifier P42566 (EPS15_HUMAN)search. The sample contained 106 residues which is < 90% of the natural sequence. Out of 106 residues 95 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 EPS15 P42566 (121-218) (EPS15_HUMAN)search Homo sapienssearch < 90% 106 89%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P42566 (121 - 218) EPS15 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH)
A Eps15 homology domain (EH domain)search EF-handsearch

Chain ID Molecular function (GO)
A (P42566) calcium ion bindingsearch

Chain InterPro annotation
A EPS15 homology (EH)search EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch