1MIR
RAT PROCATHEPSIN B
Summary for 1MIR
Entry DOI | 10.2210/pdb1mir/pdb |
Descriptor | PROCATHEPSIN B (2 entities in total) |
Functional Keywords | hydrolase, thiol protease, cysteine protease |
Biological source | Rattus norvegicus (Norway rat) |
Total number of polymer chains | 2 |
Total formula weight | 71267.25 |
Authors | Cygler, M.,Sivaraman, J.,Grochulski, P.,Coulombe, R.,Storer, A.C.,Mort, J.S. (deposition date: 1996-01-12, release date: 1997-01-11, Last modification date: 2024-10-30) |
Primary citation | Cygler, M.,Sivaraman, J.,Grochulski, P.,Coulombe, R.,Storer, A.C.,Mort, J.S. Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Structure, 4:405-416, 1996 Cited by PubMed Abstract: Cysteine proteases of the papain superfamily are synthesized as inactive precursors with a 60-110 residue N-terminal prosegment. The propeptides are potent inhibitors of their parent proteases. Although the proregion binding mode has been elucidated for all other protease classes, that of the cysteine proteases remained elusive. PubMed: 8740363DOI: 10.1016/S0969-2126(96)00046-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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