1SC9

Hydroxynitrile Lyase from Hevea brasiliensis in complex with the natural substrate acetone cyanohydrin

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1sc9a_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Hydroxynitrile lyase-like	Hydroxynitrile lyase	(Hevea brasiliensis ) [TaxId: 3981 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	alpha/beta-Hydrolases	8039822	3000102	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00561	e1sc9A1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF00561	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00561	alpha/beta hydrolase fold (Abhydrolase_1)	alpha/beta hydrolase fold	This catalytic domain is found in a very wide range of enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	(S)-acetone-cyanohydrin lyase	aliphatic (S)-hydroxynitrile lyase activity lyase activity catalytic activity hydroxynitrilase activity carbon-carbon lyase activity aldehyde-lyase activity aromatic (S)-hydroxynitrile lyase activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000073	Alpha/beta hydrolase fold-1	Domain
A	IPR045889	Methylesterase/Alpha-hydroxynitrile lyase	Family
A	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	(S)-hydroxynitrile lyase M-CSA #217	Hydroxynitrile lyases (HNLs) are important members of the alpha/beta-hydrolase superfamily, and they catalyze the cleavage of cyanohydrins into aldehyde (or ketone) and hydrocyanic acid (HCN). The release of HCN not only protects plant systems from herbivores and microbial attack, but also provides a nitrogen source for the biosynthesis of asparagine. The enzyme from Hevea brasiliensis tolerates aliphatic (including alpha,beta-unsaturated), aromatic and heterocyclic aldehydes, whereas the enzyme from Manihot esculenta catalyses the addition of hydrogen cyanide to aliphatic, aromatic, heteroaromatic aldehydes and methyl ketones. Both are specific to the S enantiomer. The overall reaction catalysed is very reversible and of importance to synthetic organic chemists.	Defined by 6 residues: THR:A-11SER:A-80CYS:A-81ASP:A-207HIS:A-235LYS:A-236 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.1.2.39 (PDB Primary Data) Search M-CSA Motif + EC 4.1.2.39

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.