1uzq Summary

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INTEGRIN BINDING CBEGF22-TB4-CBEGF33 FRAGMENT OF HUMAN FIBRILLIN-1, APO FORM CBEGF23 DOMAIN ONLY.

The structure was published by Lee, S.S.J., Knott, V., Jovanovi, J., et al., Mardon, H., Stuart, D.I., and Handford, P.A., in 2004 in a paper entitled "Structure of the Integrin Binding Fragment from Fibrillin-1 Gives New Insights Into Microfibril Organization" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2004.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of FIBRILLIN-1. This molecule has the UniProt identifier P35555 (FBN1_HUMAN)search. The sample contained 162 residues which is < 90% of the natural sequence. Out of 162 residues 152 were observed and are deposited in the PDB.

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 (1486-1647) (FBN1_HUMAN)search Homo sapienssearch < 90% 162 93%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P35555 (1486 - 1647) FIBRILLIN-1 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A EGF-type modulesearch, TB module/8-cys domainsearch Lamininsearch TB domainsearch, Calcium-binding EGF domainsearch

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

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