2w86 Summary



The structure was published by Jensen, S.A., Iqbal, S., Lowe, E.D., Redfield, C., and Handford, P.A., in 2009 in a paper entitled "Structure and Interdomain Interactions of a Hybrid Domain: A Disulphide-Rich Module of the Fibrillin/Ltbp Superfamily of Matrix Proteins." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2009.

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

The PDB entry contains the structure of FIBRILLIN-1.

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-1 P35555 (807-951) (FBN1_HUMAN)search Homo sapienssearch < 90% 147 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P35555 (807 - 951) FIBRILLIN-1 Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A Lamininsearch TB domainsearch, Calcium-binding EGF domainsearch

Chain ID Cellular component (GO) Molecular function (GO)
A (P35555) proteinaceous extracellular matrixsearch calcium ion bindingsearch extracellular matrix structural constituentsearch

Chain InterPro annotation
A EGF-type aspartate/asparagine hydroxylation sitesearch Epidermal growth factor-like domainsearch EGF-like calcium-binding domainsearch Fibrillin/Microneme protein4search TB domainsearch EGF-like calcium-binding, conserved sitesearch