1CPB | pdb_00001cpb

STRUCTURE OF CARBOXYPEPTIDASE B AT 2.8 ANGSTROMS RESOLUTION

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1cpb.1	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	Pancreatic carboxypeptidases	Carboxypeptidase B	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
B	d1cpb.1	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	Pancreatic carboxypeptidases	Carboxypeptidase B	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B	PF00246	Zinc carboxypeptidase (Peptidase_M14)	Zinc carboxypeptidase		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CARBOXYPEPTIDASE B	peptidase activity catalytic activity, acting on a protein metallocarboxypeptidase activity hydrolase activity metallopeptidase activity exopeptidase activity catalytic activity metalloexopeptidase activity carboxypeptidase activity cation binding transition metal ion binding zinc ion binding ion binding binding peptidase activity catalytic activity, acting on a protein metallocarboxypeptidase activity hydrolase activity metallopeptidase activity exopeptidase activity catalytic activity metalloexopeptidase activity carboxypeptidase activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure cytoplasmic vesicle organelle intracellular vesicle cytoplasm intracellular membrane-bounded organelle vesicle extracellular region extracellular space
B	CARBOXYPEPTIDASE B	peptidase activity catalytic activity, acting on a protein metallocarboxypeptidase activity hydrolase activity metallopeptidase activity exopeptidase activity catalytic activity metalloexopeptidase activity carboxypeptidase activity cation binding transition metal ion binding zinc ion binding ion binding binding peptidase activity catalytic activity, acting on a protein metallocarboxypeptidase activity hydrolase activity metallopeptidase activity exopeptidase activity catalytic activity metalloexopeptidase activity carboxypeptidase activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure cytoplasmic vesicle organelle intracellular vesicle cytoplasm intracellular membrane-bounded organelle vesicle extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR034253	Carboxypeptidase B, carboxypeptidase domain	Domain
A	IPR036990	Metallocarboxypeptidase-like, propeptide	Homologous Superfamily
A	IPR003146	Carboxypeptidase, activation peptide	Domain
A	IPR000834	Peptidase M14, carboxypeptidase A	Domain
B	IPR034253	Carboxypeptidase B, carboxypeptidase domain	Domain
B	IPR036990	Metallocarboxypeptidase-like, propeptide	Homologous Superfamily
B	IPR003146	Carboxypeptidase, activation peptide	Domain
B	IPR000834	Peptidase M14, carboxypeptidase A	Domain

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.