1emn Summary

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NMR STUDY OF A PAIR OF FIBRILLIN CA2+ BINDING EPIDERMAL GROWTH FACTOR-LIKE DOMAINS, MINIMIZED AVERAGE STRUCTURE

The structure was published by Downing, A.K., Knott, V., Werner, J.M., Cardy, C.M., Campbell, I.D., and Handford, P.A., in 1996 in a paper entitled "Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1996.

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

The PDB entry contains the structure of FIBRILLIN. This molecule has the UniProt identifier P35555 (FBN1_HUMAN)search. The sample contained 82 residues which is < 90% of the natural sequence. Out of 82 residues 82 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 FIBRILLIN P35555 (2124-2205) (FBN1_HUMAN)search Homo sapienssearch < 90% 82 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P35555 (2124 - 2205) FIBRILLIN Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A EGF-type modulesearch Calcium-binding EGF domainsearch
Chain InterPro annotation
A EGF-type aspartate/asparagine hydroxylation sitesearch Epidermal growth factor-like domainsearch EGF-like calcium-binding domainsearch Insulin-like growth factor binding protein, N-terminalsearch Fibrillin/Microneme protein4search EGF-like, conserved sitesearch EGF-like calcium-binding, conserved sitesearch