4AR9

Crystal structure of the peptidase domain of collagenase T from Clostridium tetani at 1.69 angstrom resolution.

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF18496	e4ar9A3	A: a+b two layers	X: Alpha-beta plaits	H: Collagenase G catalytic helper subdomain (From Topology)	T: Collagenase G catalytic helper subdomain	F: PF18496	ECOD (1.6)
A	PF01752	e4ar9A1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01752	ECOD (1.6)
B	PF18496	e4ar9B3	A: a+b two layers	X: Alpha-beta plaits	H: Collagenase G catalytic helper subdomain (From Topology)	T: Collagenase G catalytic helper subdomain	F: PF18496	ECOD (1.6)
B	PF01752	e4ar9B2	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01752	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.30.160	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Collagenase ColT, N-terminal domain	CATH (4.3.0)
A	1.10.390.20	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
A	3.30.980.50	Alpha Beta	2-Layer Sandwich	Threonyl-tRNA Synthetase	Chain A, domain 2	CATH (4.3.0)
B	3.40.30.160	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Collagenase ColT, N-terminal domain	CATH (4.3.0)
B	1.10.390.20	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
B	3.30.980.50	Alpha Beta	2-Layer Sandwich	Threonyl-tRNA Synthetase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF18496	Collagenase G catalytic helper subdomain (ColG_sub)	Collagenase G catalytic helper subdomain	This is the catalytic helper subdomain found in collagenase G from Clostridium histolyticum. This domain is indispensable for proper folding and full peptidase activity [1, 2].	Domain
A, B	PF01752	Collagenase (Peptidase_M9)	Collagenase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	COLLAGENASE COLT	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding transition metal ion binding zinc ion binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity endopeptidase activity metalloendopeptidase activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding transition metal ion binding zinc ion binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity endopeptidase activity metalloendopeptidase activity metallopeptidase activity	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR041379	Collagenase ColG-like, catalytic helper subdomain	Domain
A, B	IPR007280	Peptidase, C-terminal, archaeal/bacterial	Domain
A, B	IPR002169	Peptidase M9A/M9B, collagenase, bacterial	Family
A, B	IPR013661	Peptidase M9, collagenase, N-terminal domain	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 R01GM133198.