1QRZ
CATALYTIC DOMAIN OF PLASMINOGEN
Summary for 1QRZ
| Entry DOI | 10.2210/pdb1qrz/pdb |
| Descriptor | PLASMINOGEN (2 entities in total) |
| Functional Keywords | microplasminogen, serine protease, zymogen, chymotrypsin family, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P00747 |
| Total number of polymer chains | 4 |
| Total formula weight | 108080.06 |
| Authors | Peisach, E.,Wang, J.,de los Santos, T.,Reich, E.,Ringe, D. (deposition date: 1999-06-16, release date: 1999-10-14, Last modification date: 2024-11-06) |
| Primary citation | Peisach, E.,Wang, J.,de los Santos, T.,Reich, E.,Ringe, D. Crystal structure of the proenzyme domain of plasminogen. Biochemistry, 38:11180-11188, 1999 Cited by PubMed Abstract: We have solved the X-ray crystal structure of the proenzyme form of the catalytic domain of plasminogen, with the nonessential mutations M585Q, V673M, and M788L, to 2.0 A resolution. The structure presents an inactive protease characterized by Asp740 (chymotrypsinogen 194) hydrogen bonded to His586 (chymotrypsinogen 40), preventing proper formation of the oxyanion hole and S1 specificity pocket. In addition, the catalytic triad residues are misplaced relative to the active conformation adopted by serine proteases in the chymotrypsin family. Finally, a unique form of zymogen inactivation is observed, characterized by a "foot-in-mouth" mechanism in which Trp761 (chymotrypsinogen 215) is folded into the S1 specificity pocket preventing substrate binding. PubMed: 10460175DOI: 10.1021/bi991130r PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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