1GOI
Crystal structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution
Summary for 1GOI
Entry DOI | 10.2210/pdb1goi/pdb |
Related | 1E15 1E6N 1E6P 1E6R 1E6Z |
Descriptor | CHITINASE B, GLYCEROL, SULFATE ION, ... (4 entities in total) |
Functional Keywords | chitin degradation, hydrolase, glycosidase |
Biological source | SERRATIA MARCESCENS |
Total number of polymer chains | 2 |
Total formula weight | 112523.43 |
Authors | Kolstad, G.,Synstad, B.,Eijsink, V.G.H.,Van Aalten, D.M.F. (deposition date: 2001-10-21, release date: 2001-11-15, Last modification date: 2024-10-23) |
Primary citation | Kolstad, G.,Synstad, B.,Eijsink, V.G.H.,Van Aalten, D.M.F. Structure of the D140N Mutant of Chitinase B from Serratia Marcescens at 1.45 A Resolution. Acta Crystallogr.,Sect.D, 58:377-, 2002 Cited by PubMed Abstract: The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis. PubMed: 11807282DOI: 10.1107/S0907444901018972 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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