1qj4 Summary



The structure was published by Gruber, K., Gugganig, M., Wagner, U.G., and Kratky, C., in 1999 in a paper entitled "Atomic Resolution Crystal Structure of Hydroxynitrile Lyase from Hevea Brasiliensis" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.1 Å and deposited in 1999.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of HYDROXYNITRILE LYASE. This molecule has the UniProt identifier P52704 (HNL_HEVBR)search. The sample contained 257 residues which is 100% of the natural sequence. Out of 257 residues 255 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 most likely forms homodimers.

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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A HYDROXYNITRILE LYASE P52704 (1-257) (HNL_HEVBR)search Hevea brasiliensissearch 100% 257 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P52704 (1 - 257) HYDROXYNITRILE LYASE Hevea brasiliensis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P52704) Hydroxynitrile lyase-likesearch Rossmann foldsearch PF12697: Alpha/beta hydrolase familysearch

Chain ID Molecular function (GO) Biological process (GO)
A (P52704) aromatic (S)-hydroxynitrile lyase activitysearch aliphatic (S)-hydroxynitrile lyase activitysearch lyase activitysearch metabolic processsearch

Chain InterPro annotation
A Alpha/Beta hydrolase foldsearch