2wor Summary

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CO-STRUCTURE OF S100A7 WITH 1,8 ANS

The structure was published by Leon, R., Murray, J.I., Cragg, G., et al., Bohne, C., Boulanger, M.J., and Hof, F., in 2009 in a paper entitled "Identification and Characterization of Binding Sites on S100A7, a Participant in Cancer and Inflammation Pathways." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 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 100 residues which is 99% of the natural sequence. Out of 100 residues 96 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 (2-101) (S10A7_HUMAN)search Homo sapienssearch 95% 100 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P31151 (2 - 101) 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 Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P31151) cytoplasmsearch endoplasmic reticulumsearch focal adhesionsearch extracellular regionsearch cytosolsearch extracellular vesicular exosomesearch nucleussearch positive regulation of monocyte chemotaxissearch response to lipopolysaccharidesearch sequestering of metal ionsearch angiogenesissearch positive regulation of T cell chemotaxissearch epidermis developmentsearch defense response to Gram-negative bacteriumsearch positive regulation of ERK1 and ERK2 cascadesearch response to reactive oxygen speciessearch innate immune responsesearch keratinocyte differentiationsearch positive regulation of granulocyte chemotaxissearch calcium ion bindingsearch protein bindingsearch metal ion bindingsearch zinc ion bindingsearch RAGE receptor bindingsearch

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