Hydroxynitrile Lyase from Hevea brasiliensis in complex with the natural substrate acetone cyanohydrin
The structure was published by Gruber, K., Gartler, G., Krammer, B., Schwab, H., and Kratky, C., in 2004 in a paper entitled "Reaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily: the three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of (S)-acetone-cyanohydrin lyase. This molecule has the UniProt identifier P52704 (HNL_HEVBR). The sample contained 257 residues which is 100% of the natural sequence. Out of 257 residues 256 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: