1P57
Extracellular domain of human hepsin
Summary for 1P57
| Entry DOI | 10.2210/pdb1p57/pdb |
| Descriptor | Serine protease hepsin, 2-{5-[AMINO(IMINIO)METHYL]-1H-BENZIMIDAZOL-2-YL}BENZENOLATE, ... (4 entities in total) |
| Functional Keywords | srcr, scavenger receptor cysteine-rich domain, serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell membrane ; Single-pass type II membrane protein : P05981 P05981 |
| Total number of polymer chains | 2 |
| Total formula weight | 40347.68 |
| Authors | Somoza, J.R.,Ho, J.D.,Luong, C.,Sprengeler, P.A.,Mortara, K.,Shrader, W.D.,Sperandio, D.,Chan, H.,McGrath, M.E.,Katz, B.A. (deposition date: 2003-04-25, release date: 2004-01-20, Last modification date: 2024-10-30) |
| Primary citation | Somoza, J.R.,Ho, J.D.,Luong, C.,Ghate, M.,Sprengeler, P.A.,Mortara, K.,Shrader, W.D.,Sperandio, D.,Chan, H.,McGrath, M.E.,Katz, B.A. The Structure of the Extracellular Region of Human Hepsin Reveals a Serine Protease Domain and a Novel Scavenger Receptor Cysteine-Rich (SRCR) Domain Structure, 11:1123-1131, 2003 Cited by PubMed Abstract: Hepsin is an integral membrane protein that may participate in cell growth and in maintaining proper cell morphology and is overexpressed in a number of primary tumors. We have determined the 1.75 A resolution structure of the extracellular component of human hepsin. This structure includes a 255-residue trypsin-like serine protease domain and a 109-residue region that forms a novel, poorly conserved, scavenger receptor cysteine-rich (SRCR) domain. The two domains are associated with each other through a single disulfide bond and an extensive network of noncovalent interactions. The structure suggests how the extracellular region of hepsin may be positioned with respect to the plasma membrane. PubMed: 12962630DOI: 10.1016/S0969-2126(03)00148-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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