1L9M

Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1l9ma2	All beta proteins	Immunoglobulin-like beta-sandwich	Transglutaminase, two C-terminal domains	Transglutaminase, two C-terminal domains	Transglutaminase, two C-terminal domains	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1l9ma1	All beta proteins	Immunoglobulin-like beta-sandwich	E set domains	Transglutaminase N-terminal domain	Transglutaminase N-terminal domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1l9ma4	Alpha and beta proteins (a+b)	Cysteine proteinases	Cysteine proteinases	Transglutaminase core	Transglutaminase catalytic domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1l9mb2	All beta proteins	Immunoglobulin-like beta-sandwich	Transglutaminase, two C-terminal domains	Transglutaminase, two C-terminal domains	Transglutaminase, two C-terminal domains	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1l9mb1	All beta proteins	Immunoglobulin-like beta-sandwich	E set domains	Transglutaminase N-terminal domain	Transglutaminase N-terminal domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1l9mb4	Alpha and beta proteins (a+b)	Cysteine proteinases	Cysteine proteinases	Transglutaminase core	Transglutaminase catalytic domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cysteine proteinases	8041161	3001808	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	E set domains	8055035	3000070	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CsgC/transglutaminase domain-like	8055227	3002048	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CsgC/transglutaminase domain-like	8055478	3002048	SCOP2B (2022-06-29)
B	SCOP2 Family	Transglutaminase core	8028782	4000877	SCOP2 (2022-06-29)
B	SCOP2 Family	Transglutaminase N-terminal domain	8055034	4007520	SCOP2 (2022-06-29)
B	SCOP2 Family	Transglutaminase, two C-terminal domains	8055226	4007533	SCOP2 (2022-06-29)
B	SCOP2 Family	Transglutaminase, two C-terminal domains	8055477	4007533	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Cysteine proteinases	8041161	3001808	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	E set domains	8055035	3000070	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	CsgC/transglutaminase domain-like	8055227	3002048	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	CsgC/transglutaminase domain-like	8055478	3002048	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Transglut_N	e1l9mA5	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_N	ECOD (1.6)
A	Transglut_C_1	e1l9mA6	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_C_1	ECOD (1.6)
A	Transglut_C	e1l9mA7	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_C	ECOD (1.6)
A	Transglut_core	e1l9mA8	A: a+b complex topology	X: Cysteine proteinases-like	H: Cysteine proteinases (From Topology)	T: Cysteine proteinases	F: Transglut_core	ECOD (1.6)
B	Transglut_N	e1l9mB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_N	ECOD (1.6)
B	Transglut_C_1	e1l9mB6	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_C_1	ECOD (1.6)
B	Transglut_C	e1l9mB3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_C	ECOD (1.6)
B	Transglut_core	e1l9mB5	A: a+b complex topology	X: Cysteine proteinases-like	H: Cysteine proteinases (From Topology)	T: Cysteine proteinases	F: Transglut_core	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
A	3.90.260.10	Alpha Beta	Alpha-Beta Complex	Coagulation Factor XIII	Chain A, domain 2	CATH (4.3.0)
B	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
B	3.90.260.10	Alpha Beta	Alpha-Beta Complex	Coagulation Factor XIII	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00868	Transglutaminase family (Transglut_N)	Transglutaminase family		Domain
A, B	PF00927	Transglutaminase family, C-terminal ig like domain (Transglut_C)	Transglutaminase family, C-terminal ig like domain		Domain
A, B	PF01841	Transglutaminase-like superfamily (Transglut_core)	Transglutaminase-like superfamily	This domain is found in animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that ...	This domain is found in animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterised transglutaminase, the human blood clotting factor XIIIa' [1]. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase [2], it is proposed that many, if not all, microbial homologues of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease. [3]	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Protein-glutamine glutamyltransferase E3	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding aminoacyltransferase activity protein-glutamine gamma-glutamyltransferase activity catalytic activity, acting on a protein acyltransferase activity transferase activity catalytic activity structural molecule activity	developmental process epithelium development epidermal cell differentiation cellular developmental process epidermis development animal organ development tissue development epithelial cell differentiation skin development cell differentiation keratinocyte differentiation anatomical structure development cellular process macromolecule modification developmental process epithelium development epidermal cell differentiation cellular developmental process epidermis development animal organ development tissue development epithelial cell differentiation skin development cell differentiation keratinocyte differentiation anatomical structure development cellular process macromolecule modification metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process multicellular organismal process molting cycle process hair cycle epidermis morphogenesis morphogenesis of an epithelium tissue morphogenesis anatomical structure morphogenesis skin epidermis development hair follicle development molting cycle hair cycle process hair follicle morphogenesis keratinization peptide cross-linking	extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm protein-containing complex cell periphery extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm protein-containing complex cell periphery extrinsic component of plasma membrane cytoplasmic side of plasma membrane cytoplasmic side of membrane membrane plasma membrane extrinsic component of membrane extrinsic component of cytoplasmic side of plasma membrane side of membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036985	Transglutaminase-like superfamily	Homologous Superfamily
A, B	IPR036238	Transglutaminase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR002931	Transglutaminase-like	Domain
A, B	IPR014756	Immunoglobulin E-set	Homologous Superfamily
A, B	IPR038765	Papain-like cysteine peptidase superfamily	Homologous Superfamily
A, B	IPR001102	Transglutaminase, N-terminal	Domain
A, B	IPR008958	Transglutaminase, C-terminal	Domain
A, B	IPR050779	Protein-glutamine gamma-glutamyltransferases	Family
A, B	IPR023608	Protein-glutamine gamma-glutamyltransferase, animal	Family
A, B	IPR013808	Transglutaminase, active site	Active Site
A, B	IPR013783	Immunoglobulin-like fold	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: Q08188	skin basal cell carcinoma uncombable hair syndrome esophageal adenocarcinoma uncombable hair syndrome 2 hepatocellular carcinoma psoriasis uncombable hair syndrome 1

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.