5CHA

THE REFINEMENT AND THE STRUCTURE OF THE DIMER OF ALPHA-CHYMOTRYPSIN AT 1.67-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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5cha.1	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	(alpha,gamma)-chymotrypsin(ogen)	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
D [auth E]	d5cha.2	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	(alpha,gamma)-chymotrypsin(ogen)	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
B	d5cha.1	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	(alpha,gamma)-chymotrypsin(ogen)	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
E [auth F]	d5cha.2	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	(alpha,gamma)-chymotrypsin(ogen)	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
F [auth G]	d5cha.2	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	(alpha,gamma)-chymotrypsin(ogen)	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
C	d5cha.1	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	(alpha,gamma)-chymotrypsin(ogen)	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
E [auth F]	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
F [auth G]	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
C	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, E [auth F]	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
C, F [auth G]	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, D [auth E]	ALPHA-CHYMOTRYPSIN A	peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity protein binding binding serpin family protein binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process multicellular organismal process digestion	protein-containing complex serine protease inhibitor complex protease inhibitor complex peptidase inhibitor complex cellular anatomical structure extracellular region
B, E [auth F]	ALPHA-CHYMOTRYPSIN A	peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity protein binding binding serpin family protein binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process multicellular organismal process digestion	protein-containing complex serine protease inhibitor complex protease inhibitor complex peptidase inhibitor complex cellular anatomical structure extracellular region
C, F [auth G]	ALPHA-CHYMOTRYPSIN A	peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity protein binding binding serpin family protein binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process multicellular organismal process digestion	protein-containing complex serine protease inhibitor complex protease inhibitor complex peptidase inhibitor complex cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, D [auth E]	IPR001254	Serine proteases, trypsin domain	Domain
A, D [auth E]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A, D [auth E]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A, D [auth E]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A, D [auth E]	IPR001314	Peptidase S1A, chymotrypsin family	Family
A, D [auth E]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
B, E [auth F]	IPR001254	Serine proteases, trypsin domain	Domain
B, E [auth F]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
B, E [auth F]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
B, E [auth F]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
B, E [auth F]	IPR001314	Peptidase S1A, chymotrypsin family	Family
B, E [auth F]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
C, F [auth G]	IPR001254	Serine proteases, trypsin domain	Domain
C, F [auth G]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
C, F [auth G]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
C, F [auth G]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
C, F [auth G]	IPR001314	Peptidase S1A, chymotrypsin family	Family
C, F [auth G]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site

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.