4ARF
CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE H FROM CLOSTRIDIUM HISTOLYTICUM IN COMPLEX WITH THE PEPTIDIC INHIBITOR ISOAMYLPHOSPHONYL-GLY-PRO-ALA AT 1.77 ANGSTROM RESOLUTION.
Summary for 4ARF
Entry DOI | 10.2210/pdb4arf/pdb |
Related | 4AR1 |
Descriptor | COLH PROTEIN, ISOAMYLPHOSPHONYL-GLY-PRO-ALA, ZINC ION, ... (5 entities in total) |
Functional Keywords | hydrolase-inhibitor complex, collagenolysis, hydrolyse, metalloprotease, hexxh, hydrolase/inhibitor |
Biological source | CLOSTRIDIUM HISTOLYTICUM More |
Total number of polymer chains | 2 |
Total formula weight | 46373.66 |
Authors | Eckhard, U.,Brandstetter, H. (deposition date: 2012-04-23, release date: 2013-06-05, Last modification date: 2023-12-20) |
Primary citation | Eckhard, U.,Schonauer, E.,Brandstetter, H. Structural Basis for Activity Regulation and Substrate Preference of Clostridial Collagenases G, H, and T. J.Biol.Chem., 288:20184-, 2013 Cited by PubMed: 23703618DOI: 10.1074/JBC.M112.448548 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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