1WHS

STRUCTURE OF THE COMPLEX OF L-BENZYLSUCCINATE WITH WHEAT SERINE CARBOXYPEPTIDASE II AT 2.0 ANGSTROMS RESOLUTION

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)
A	d1whs.1	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Serine carboxypeptidase-like	Serine carboxypeptidase II	common wheat (Triticum aestivum ) [TaxId: 4565 ],	SCOPe (2.08)
B	d1whs.1	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Serine carboxypeptidase-like	Serine carboxypeptidase II	common wheat (Triticum aestivum ) [TaxId: 4565 ],	SCOPe (2.08)

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)
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	PF00450	Serine carboxypeptidase (Peptidase_S10)	Serine carboxypeptidase	-	Domain
B	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	SERINE CARBOXYPEPTIDASE II	serine-type exopeptidase activity peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type carboxypeptidase activity serine-type peptidase activity hydrolase activity exopeptidase activity catalytic activity carboxypeptidase activity	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	-
B	SERINE CARBOXYPEPTIDASE II	serine-type exopeptidase activity peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type carboxypeptidase activity serine-type peptidase activity hydrolase activity exopeptidase activity catalytic activity carboxypeptidase activity	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001563	Peptidase S10, serine carboxypeptidase	Family
A	IPR018202	Serine carboxypeptidase, serine active site	Active Site
A	IPR033124	Serine carboxypeptidases, histidine active site	Active Site
A	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
B	IPR001563	Peptidase S10, serine carboxypeptidase	Family
B	IPR018202	Serine carboxypeptidase, serine active site	Active Site
B	IPR033124	Serine carboxypeptidases, histidine active site	Active Site
B	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, B	carboxypeptidase D M-CSA #5	Carboxypeptidase D is a serine protease which specifically removes basic or hydrophobic residues from the C-terminus of the substrate protein. Carboxypeptidase D is a member of the alpha beta hydrolase family and contains a Ser-His-Asp catalytic triad typical of the family. In humans, mutations arising in this enzyme result in genetic disorders such as galactosialidosis, a disease associated with incorrect protein degradation in the lysosome. Carboxypeptidase D from yeast and wheat have had their structures determined, The wheat catalytic triad is made up of residues from both subunits of the homodimer whilst yeast carboxypeptidase D is a monomer, however, both have similar active site geometries.	Defined by 5 residues: GLY:A-57 [auth A-53]SER:A-153 [auth A-146]TYR:A-154 [auth A-147]ASP:B-75 [auth B-338]HIS:B-127 [auth B-397] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.4.16.1 (PDB Primary Data) Search M-CSA Motif + EC 3.4.16.1

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.