1QJ4
HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION
Summary for 1QJ4
| Entry DOI | 10.2210/pdb1qj4/pdb |
| Related | 1YAS |
| Descriptor | HYDROXYNITRILE LYASE, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | oxynitrilase, cyanogenesis, cyanhydrin formation, lyase |
| Biological source | HEVEA BRASILIENSIS (PARA RUBBER TREE) |
| Total number of polymer chains | 1 |
| Total formula weight | 29738.94 |
| Authors | Gugganig, M.,Gruber, K.,Kratky, C. (deposition date: 1999-06-21, release date: 1999-10-10, Last modification date: 2023-12-13) |
| Primary citation | Gruber, K.,Gugganig, M.,Wagner, U.G.,Kratky, C. Atomic Resolution Crystal Structure of Hydroxynitrile Lyase from Hevea Brasiliensis Biol.Chem., 380:993-, 1999 Cited by PubMed Abstract: The X-ray crystal structure of native hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL) has been determined at 1.1 A resolution. It refined to a final R of 11.5% for all data and an Rfree of 14.4%. The favorable data-to-parameter ratio at atomic resolution made the refinement of individual anisotropic displacement parameters possible. The data also allowed a clear distinction of the alternate orientations of all histidine and the majority of asparagine and glutamine side chains. A number of hydrogen atoms, including one on the imidazole of the mechanistically important His-235, became visible as peaks in a difference electron density map. The structure revealed a discretely disordered sidechain of Ser-80, which is part of the putative catalytic triad. Analysis of the anisotropy indicated an increased mobility of residues near the entrance to the active site and within the active site. PubMed: 10494852DOI: 10.1515/BC.1999.123 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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