Annotations: 6QIG

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth L]	d6qigl2	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	C1 set domains (antibody constant domain-like)	automated matches	(Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A [auth L]	d6qigl1	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	automated matches	automated matches	(Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
B [auth H]	d6qigh_	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	V set domains (antibody variable domain-like)	automated matches	(Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth L]	PF07654	e6qigL1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF07654	ECOD (1.6)
A [auth L]	PF07686	e6qigL2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF07686	ECOD (1.6)
B [auth H]	PF07654	e6qigH2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF07654	ECOD (1.6)
B [auth H]	PF07686	e6qigH1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF07686	ECOD (1.6)
C [auth A]	PF05986	e6qigA2	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in ADAMTS13 (From Topology)	T: Jelly-roll domain in ADAMTS13	F: PF05986	ECOD (1.6)
C [auth A]	PF01421	e6qigA1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01421	ECOD (1.6)
C [auth A]	PF19236	e6qigA3	A: few secondary structure elements	X: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins (From Topology)	H: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins (From Topology)	T: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins	F: PF19236	ECOD (1.6)
C [auth A]	PF17771	e6qigA5	A: few secondary structure elements	X: Blood coagulation inhibitor (disintegrin) (From Topology)	H: Blood coagulation inhibitor (disintegrin) (From Topology)	T: Blood coagulation inhibitor (disintegrin)	F: PF17771	ECOD (1.6)
C [auth A]	PF00090	e6qigA4	A: few secondary structure elements	X: TSP-1 type 1 repeat (From Topology)	H: TSP-1 type 1 repeat (From Topology)	T: TSP-1 type 1 repeat	F: PF00090	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth L]	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (utative)
B [auth H]	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (utative)

IMGT Antibody Annotation IMGT Database Homepage

Chain	Protein Name	Description	Organism Name	Gene Allele Name(s)	Domain Name(s)	Receptor Type	Receptor Description	Provenance Source
A [auth L]	Antibody Fab Fragment	L-KAPPA	Mus musculus (house mouse)	IGKV5-4501, IGKJ401, IGKJ402, IGKJ301, IGKC01, IGKC02	V-DOMAIN V-KAPPA, C-DOMAIN C-KAPPA	IG	FAB-GAMMA-1_KAPPA	IMGT (202416-0)
B [auth H]	Antibody Fab Fragment	VH-CH1	Mus musculus (house mouse)	IGHV5-6-101, IGHV5-601, IGHJ401, IGHG102	V-DOMAIN VH, C-DOMAIN CH1	IG	FAB-GAMMA-1_KAPPA	IMGT (202416-0)

SAbDab Antibody Annotation SAbDab Database Homepage

Chain	Chain Class	Chain Subclass	Chain Type	Antigen Name(s)	Provenance Source
A [auth L]	Light Chain	IGKV5	Kappa	a disintegrin and metalloproteinase with thrombospondinmotifs 13	SAbDab (2024-04-26)
B [auth H]	Heavy Chain	IGHV5	-	a disintegrin and metalloproteinase with thrombospondinmotifs 13	SAbDab (2024-04-26)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
C [auth A]	PF00090	Thrombospondin type 1 domain (TSP_1)	Thrombospondin type 1 domain	-	Domain
C [auth A]	PF19236	ADAMTS cysteine-rich domain (ADAMTS_CR_3)	ADAMTS cysteine-rich domain	This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals [1,2]. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues [3]. ADAM-TS (A Disintegrin and Metalloproteinase w ...	This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals [1,2]. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues [3]. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, Pfam:PF08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organisation [4,5]. Members of the ADAMTS family have been implicated in a range of diseases [1,6,7].	Domain
C [auth A]	PF17771	ADAMTS cysteine-rich domain 2 (ADAMTS_CR_2)	ADAMTS cysteine-rich domain 2	This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (Pfam:PF08516) [1,2]. Members of the ADAM-TS family have been implicated ...	This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (Pfam:PF08516) [1,2]. Members of the ADAM-TS family have been implicated in a range of diseases [3,4,5]. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity [6].	Domain
C [auth A]	PF01421	Reprolysin (M12B) family zinc metalloprotease (Reprolysin)	Reprolysin (M12B) family zinc metalloprotease	The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammal ...	The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin Swiss:Q28472. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.	Domain
C [auth A]	PF05986	ADAM-TS Spacer 1 (ADAMTS_spacer1)	ADAM-TS Spacer 1	This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins [1]. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a s ...	This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins [1]. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organisation among its members [2,3]. Members of the ADAM-TS family have been implicated in a range of diseases [4,7]. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles [4]. Examples of ADAM-TS-like proteins are papilin [5] and punctin [6].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth L]	Antibody Light Chain	-	-	-
B [auth H]	Antibody Heavy Chain	-	-	-
C [auth A]	A disintegrin and metalloproteinase with thrombospondin motifs 13	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding metalloendopeptidase activity endopeptidase activity cell adhesion molecule binding peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding metalloendopeptidase activity endopeptidase activity cell adhesion molecule binding protein-containing complex binding protein binding integrin binding signaling receptor binding transition metal ion binding zinc ion binding	cell adhesion cell-matrix adhesion cell-substrate adhesion cellular process cellular catabolic process organic substance metabolic process catabolic process cellular metabolic process metabolic process organic substance catabolic process peptide metabolic process peptide catabolic process cellular response to stimulus response to organic substance cell adhesion cell-matrix adhesion cell-substrate adhesion cellular process cellular catabolic process organic substance metabolic process catabolic process cellular metabolic process metabolic process organic substance catabolic process peptide metabolic process peptide catabolic process cellular response to stimulus response to organic substance response to stimulus response to cytokine response to interleukin-4 cellular response to chemical stimulus response to chemical cellular response to cytokine stimulus cellular response to interleukin-4 cellular response to organic substance cellular component organization extracellular matrix organization cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization regulation of biological process integrin-mediated signaling pathway regulation of cellular process cell surface receptor signaling pathway signaling biological regulation cell communication signal transduction organonitrogen compound catabolic process organonitrogen compound metabolic process primary metabolic process protein catabolic process macromolecule catabolic process protein metabolic process macromolecule metabolic process biological process involved in interspecies interaction between organisms response to lipid response to other organism cellular response to lipopolysaccharide response to oxygen-containing compound response to external stimulus cellular response to molecule of bacterial origin response to lipopolysaccharide cellular response to oxygen-containing compound response to biotic stimulus cellular response to biotic stimulus response to bacterium cellular response to lipid response to external biotic stimulus response to molecule of bacterial origin response to potassium ion response to metal ion response to inorganic substance cellular biosynthetic process gene expression macromolecule biosynthetic process protein maturation biosynthetic process proteolysis organic substance biosynthetic process protein processing response to toxic substance carbohydrate derivative metabolic process glycoprotein metabolic process multicellular organismal process regulation of body fluid levels wound healing cell activation hemostasis blood coagulation response to stress coagulation regulation of biological quality response to wounding platelet activation cellular response to tumor necrosis factor response to tumor necrosis factor response to type II interferon cellular response to type II interferon innate immune response immune response defense response defense response to symbiont immune system process defense response to other organism response to amine response to organonitrogen compound response to nitrogen compound	cell surface cellular anatomical entity cell periphery extracellular matrix external encapsulating structure membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen endoplasmic reticulum lumen intracellular organelle organelle lumen cell surface cellular anatomical entity cell periphery extracellular matrix external encapsulating structure membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen endoplasmic reticulum lumen intracellular organelle organelle lumen organelle endoplasmic reticulum cytoplasm extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
C [auth A]	IPR013273	ADAMTS/ADAMTS-like	Family
C [auth A]	IPR001590	Peptidase M12B, ADAM/reprolysin	Domain
C [auth A]	IPR035914	Spermadhesin, CUB domain superfamily	Homologous Superfamily
C [auth A]	IPR000884	Thrombospondin type-1 (TSP1) repeat	Repeat
C [auth A]	IPR041645	ADAMTS, cysteine-rich domain 2	Domain
C [auth A]	IPR010294	ADAMTS/ADAMTS-like, Spacer 1	Domain
C [auth A]	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
C [auth A]	IPR036383	Thrombospondin type-1 (TSP1) repeat superfamily	Homologous Superfamily
C [auth A]	IPR045371	ADAMTS/ADAMTS-like, cysteine-rich domain 3	Domain
C [auth A]	IPR006586	ADAM, cysteine-rich domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
C [auth A]	Pharos: Q76LX8	thrombotic thrombocytopenic purpura congenital thrombotic thrombocytopenic purpura autoimmune thrombocytopenic purpura thrombotic microangiopathy thrombophilia anemia congenital anemia Familial Thrombotic Thrombocytopenic Purpura thrombocytopenia atypical hemolytic-uremic syndrome hepatocellular carcinoma osteosarcoma hereditary von Willebrand disease purpura thrombotic disease thrombotic thrombocytopenic purpura congenital thrombotic thrombocytopenic purpura autoimmune thrombocytopenic purpura thrombotic microangiopathy thrombophilia anemia congenital anemia Familial Thrombotic Thrombocytopenic Purpura thrombocytopenia atypical hemolytic-uremic syndrome hepatocellular carcinoma osteosarcoma hereditary von Willebrand disease purpura thrombotic disease vascular disease

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.