2DSK
Crystal structure of catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosus
Summary for 2DSK
Entry DOI | 10.2210/pdb2dsk/pdb |
Descriptor | chitinase, GLYCEROL, SULFATE ION, ... (4 entities in total) |
Functional Keywords | chitinase, catalytic domain, active domain, crystalline chitin, tim-barrel, hydrolase |
Biological source | Pyrococcus furiosus |
Total number of polymer chains | 2 |
Total formula weight | 70177.08 |
Authors | Nakamura, T.,Mine, S.,Hagihara, Y.,Ishikawa, K.,Uegaki, K. (deposition date: 2006-06-30, release date: 2007-02-06, Last modification date: 2024-03-13) |
Primary citation | Nakamura, T.,Mine, S.,Hagihara, Y.,Ishikawa, K.,Uegaki, K. Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus ACTA CRYSTALLOGR.,SECT.F, 63:7-11, 2007 Cited by PubMed Abstract: The crystal structure of the catalytic domain of a chitinase from the hyperthermophilic archaeon Pyrococcus furiosus (AD2(PF-ChiA)) has been determined at 1.5 A resolution. This is the first structure of the catalytic domain of an archaeal chitinase. The overall structure of AD2(PF-ChiA) is a TIM-barrel fold with a tunnel-like active site that is a common feature of family 18 chitinases. Although the catalytic residues (Asp522, Asp524 and Glu526) are conserved, comparison of the conserved residues and structures with those of other homologous chitinases indicates that the catalytic mechanism of PF-ChiA is different from that of family 18 chitinases. PubMed: 17183162DOI: 10.1107/S1744309106051773 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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