2wnd Summary

pdbe.org/2wnd
spacer

STRUCTURE OF AN S100A7 TRIPLE MUTANT

The structure was published by West, N.R., Farnell, B., Murray, J.I., Hof, F., Watson, P.H., and Boulanger, M.J., in 2009 in a paper entitled "Structural and Functional Characterization of a Triple Mutant Form of S100A7 Defective for Jab1 Binding." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 2009.

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

The PDB entry contains the structure of PROTEIN S100-A7. This molecule has the UniProt identifier P31151 (S10A7_HUMAN)search. The sample contained 96 residues which is 95% of the natural sequence. Out of 96 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 most likely forms homodimers.

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 PROTEIN S100-A7 P31151 (2-97) (S10A7_HUMAN)search Homo sapienssearch 95% 96 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P31151 (2 - 97) PROTEIN S100-A7 Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A (P31151) EF-handsearch PF01023: S-100/ICaBP type calcium binding domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P31151) calcium ion bindingsearch protein bindingsearch metal ion bindingsearch zinc ion bindingsearch RAGE receptor bindingsearch cytoplasmsearch extracellular regionsearch focal adhesionsearch cytosolsearch nucleussearch extracellular vesicular exosomesearch endoplasmic reticulumsearch sequestering of metal ionsearch keratinocyte differentiationsearch positive regulation of ERK1 and ERK2 cascadesearch angiogenesissearch response to reactive oxygen speciessearch response to lipopolysaccharidesearch positive regulation of T cell chemotaxissearch epidermis developmentsearch positive regulation of granulocyte chemotaxissearch positive regulation of monocyte chemotaxissearch defense response to Gram-negative bacteriumsearch innate immune responsesearch

Chain InterPro annotation
A S100/Calbindin-D9k, conserved sitesearch EF-hand domainsearch EF-hand domain pairsearch S100/CaBP-9k-type, calcium binding, subdomainsearch EF-Hand 1, calcium-binding sitesearch