2APR
STRUCTURE AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS
Replaces: 1APRSummary for 2APR
Entry DOI | 10.2210/pdb2apr/pdb |
Descriptor | RHIZOPUSPEPSIN, CALCIUM ION (3 entities in total) |
Functional Keywords | hydrolase (aspartic proteinase) |
Biological source | Rhizopus microsporus var. chinensis |
Total number of polymer chains | 1 |
Total formula weight | 34108.71 |
Authors | Suguna, K.,Davies, D.R. (deposition date: 1987-03-19, release date: 1987-07-16, Last modification date: 2017-11-29) |
Primary citation | Suguna, K.,Bott, R.R.,Padlan, E.A.,Subramanian, E.,Sheriff, S.,Cohen, G.H.,Davies, D.R. Structure and refinement at 1.8 A resolution of the aspartic proteinase from Rhizopus chinensis. J.Mol.Biol., 196:877-900, 1987 Cited by PubMed: 3316666DOI: 10.1016/0022-2836(87)90411-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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