ATOMIC RESOLUTION STRUCTURE OF HBP

File:1a7s.gif


1a7s, resolution 1.12Å

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OverviewOverview

Crystals of human heparin binding protein (HBP) diffract to 1.1 A when flash-frozen at 120 K. The atomic resolution structure has been refined anisotropically using SHELXL96. The final model of HBP consists of 221 amino-acid residues of 225 possible, three glycosylation units, one chloride ion, 15 precipitant ethanol molecules and 323 water molecules. The structure is refined to a final crystallographic R factor of 15.9% and Rfree(5%) of 18.9% using all data. A putative protein kinase C activation site has been identified, involving residues 113-120. The structure is compared to the previously determined 2.3 A resolution structure of HBP.

About this StructureAbout this Structure

1A7S is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Atomic resolution structure of human HBP/CAP37/azurocidin., Karlsen S, Iversen LF, Larsen IK, Flodgaard HJ, Kastrup JS, Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):598-609. PMID:9761855

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