1FLH

CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION

Summary for 1FLH

• Entry DOI: 10.2210/pdb1flh/pdb
• Descriptor: UROPEPSIN (2 entities in total)
• Functional Keywords: acid proteinase, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P00790
• Total number of polymer chains: 1
• Total formula weight: 34617.86

Authors

Canduri, F.,Teodoro, L.G.V.L.,Fadel, V.,Lorenzi, C.C.B.,Hial, V.,Gomes, R.A.S.,Neto, J.R.,De Azevedo Jr., W.F. (deposition date: 2000-08-14, release date: 2001-10-31, Last modification date: 2024-10-09)

Primary citation

Canduri, F.,Teodoro, L.G.,Fadel, V.,Lorenzi, C.C.,Hial, V.,Gomes, R.A.,Neto, J.R.,de Azevedo, W.F.
Structure of human uropepsin at 2.45 A resolution.
Acta Crystallogr.,Sect.D, 57:1560-1570, 2001

PubMed Abstract: The molecular structure of human uropepsin, an aspartic proteinase from the urine produced in the form of pepsinogen A in the gastric mucosa, has been determined by molecular replacement using human pepsin as the search model. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.99, b = 75.56, c = 89.90 A. Crystallographic refinement led to an R factor of 0.161 at 2.45 A resolution. The positions of 2437 non-H protein atoms in 326 residues have been determined and the model contains 143 water molecules. The structure is bilobal, consisting of two predominantly beta-sheet lobes which, as observed in other aspartic proteinases, are related by a pseudo-twofold axis. A model of the uropepsin-pepstatin complex has been constructed based on the high-resolution crystal structure of pepsin complexed with pepstatin.

PubMed: 11679720
DOI: 10.1107/S0907444901013865

Experimental method

X-RAY DIFFRACTION (2.45 Å)