2jpt Summary

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Structural changes induced in apo-s100a1 protein by the disulphide formation between its CYS85 residue and b-mercaptoethanol

The structure was published by Zhukov, I., Ejchart, A., and Bierzynski, A., in 2008 in a paper entitled "Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol" (abstract).

The structure was determined using NMR spectroscopy and deposited in 2007.

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

This PDB entry contains multiple copies of the structure of Protein S100-A1.

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-A1 P02639 (2-94) (S10A1_BOVIN)search Bos taurussearch 99% 93 100%
B Protein S100-A1 P02639 (2-94) (S10A1_BOVIN)search Bos taurussearch 99% 93 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P02639 (2 - 94) Protein S100-A1 Bos taurus

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P02639) EF-handsearch PF00036: EF handsearch, PF01023: S-100/ICaBP type calcium binding domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P02639) calcium ion bindingsearch protein bindingsearch metal ion bindingsearch regulation of heart contractionsearch

Chain InterPro annotation
A, B 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 Protein S100-A1search