1A7S
ATOMIC RESOLUTION STRUCTURE OF HBP
Summary for 1A7S
| Entry DOI | 10.2210/pdb1a7s/pdb |
| Descriptor | HEPARIN BINDING PROTEIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | serine protease homolog, endotoxin binding, heparin |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 25674.56 |
| Authors | Karlsen, S.,Iversen, L.F.,Larsen, I.K.,Flodgaard, H.J.,Kastrup, J.S. (deposition date: 1998-03-17, release date: 1999-03-23, Last modification date: 2024-11-06) |
| Primary citation | Karlsen, S.,Iversen, L.F.,Larsen, I.K.,Flodgaard, H.J.,Kastrup, J.S. Atomic resolution structure of human HBP/CAP37/azurocidin. Acta Crystallogr.,Sect.D, 54:598-609, 1998 Cited by PubMed Abstract: 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. PubMed: 9761855DOI: 10.1107/S0907444997016193 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.12 Å) |
Structure validation
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