1GXS

Crystal Structure of Hydroxynitrile Lyase from Sorghum bicolor in Complex with Inhibitor Benzoic Acid: a novel cyanogenic enzyme

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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)
C	d1gxs.2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Serine carboxypeptidase-like	Hydroxynitrile lyase	(Sorghum bicolor ) [TaxId: 4558 ],	SCOPe (2.08)
A	d1gxs.1	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Serine carboxypeptidase-like	Hydroxynitrile lyase	(Sorghum bicolor ) [TaxId: 4558 ],	SCOPe (2.08)
D	d1gxs.2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Serine carboxypeptidase-like	Hydroxynitrile lyase	(Sorghum bicolor ) [TaxId: 4558 ],	SCOPe (2.08)
B	d1gxs.1	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Serine carboxypeptidase-like	Hydroxynitrile lyase	(Sorghum bicolor ) [TaxId: 4558 ],	SCOPe (2.08)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
D	6.10.250.940	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
D	3.40.50.11320	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	6.10.250.940	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
B	3.40.50.11320	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C	PF00450	Serine carboxypeptidase (Peptidase_S10)	Serine carboxypeptidase	-	Domain
B, D	PF00450	Serine carboxypeptidase (Peptidase_S10)	Serine carboxypeptidase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	P-(S)-HYDROXYMANDELONITRILE LYASE CHAIN A	hydroxymandelonitrile lyase activity lyase activity catalytic activity carbon-carbon lyase activity aldehyde-lyase activity	-	-
B, D	P-(S)-HYDROXYMANDELONITRILE LYASE CHAIN B	hydroxymandelonitrile lyase activity lyase activity catalytic activity carbon-carbon lyase activity aldehyde-lyase activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR001563	Peptidase S10, serine carboxypeptidase	Family
A, C	IPR033124	Serine carboxypeptidases, histidine active site	Active Site
A, C	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
B, D	IPR001563	Peptidase S10, serine carboxypeptidase	Family
B, D	IPR033124	Serine carboxypeptidases, histidine active site	Active Site
B, D	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	P-(S)-hydroxymandelonitrile lyase M-CSA #382	Hydroxynitrile lyases (HNLs) constitute a diverse family of enzymes that catalyse the stereospecific cleavage of a wide range of cyanohydrins into aldehydes or ketones and hydrogen cyanide from injured tissues. It is also involved in the catabolism of the cyanogenic glycoside dhurrin. The release of HCN is a common defense of food plants against herbivores. The HNL of Sorghum bicolor (SbHNL) has no similarity to other HNLs except in function. This protein is a member of the Alpha/Beta hydrolase fold superfamily.	Defined by 2 residues: SER:A-158TRP:A-270 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.1.2.11 (PDB Primary Data) Search M-CSA Motif + EC 4.1.2.11

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 R01GM157729.