4XHC
rhamnosidase from Klebsiella oxytoca with rhamnose bound
Summary for 4XHC
| Entry DOI | 10.2210/pdb4xhc/pdb |
| Descriptor | Alpha-L-rhamnosidase, alpha-L-rhamnopyranose, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Klebsiella oxytoca |
| Total number of polymer chains | 2 |
| Total formula weight | 124125.85 |
| Authors | O'Neill, E.O.,Stevenson, C.E.M.,Patterson, M.J.,Rejzek, M.,Chauvin, A.,Lawson, D.M.,Field, R.A. (deposition date: 2015-01-05, release date: 2015-04-15, Last modification date: 2024-05-08) |
| Primary citation | O'Neill, E.C.,Stevenson, C.E.,Paterson, M.J.,Rejzek, M.,Chauvin, A.L.,Lawson, D.M.,Field, R.A. Crystal structure of a novel two domain GH78 family alpha-rhamnosidase from Klebsiella oxytoca with rhamnose bound. Proteins, 83:1742-1749, 2015 Cited by PubMed Abstract: The crystal structure of the GH78 family α-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 Å resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays α-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function. PubMed: 25846411DOI: 10.1002/prot.24807 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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