2APR

STRUCTURE AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS

Replaces:  1APR

Summary for 2APR

DescriptorRHIZOPUSPEPSIN, CALCIUM ION (3 entities in total)
Functional Keywordshydrolase (aspartic proteinase)
Biological sourceRhizopus microsporus var. chinensis
Total number of polymer chains1
Total molecular weight34108.71
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
PubMed: 3316666 (PDB entries with the same primary citation)
DOI: 10.1016/0022-2836(87)90411-6
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers30 1.2% 1.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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PDB entries from 2020-09-23