3B2Z | pdb_00003b2z

Crystal Structure of ADAMTS4 (apo form)

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
H	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8065560	3001975	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8065560	3001975	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8065560	3001975	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8065560	3001975	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8065560	3001975	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8065560	3001975	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8065560	3001975	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8065560	3001975	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
H	Reprolysin	e3b2zH1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
H	KOG3538_1st	e3b2zH2	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: KOG3538_1st	ECOD (1.6)
G	Reprolysin	e3b2zG1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
G	KOG3538_1st	e3b2zG2	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: KOG3538_1st	ECOD (1.6)
F	Reprolysin	e3b2zF1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
F	KOG3538_1st	e3b2zF2	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: KOG3538_1st	ECOD (1.6)
E	Reprolysin	e3b2zE1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
E	KOG3538_1st	e3b2zE2	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: KOG3538_1st	ECOD (1.6)
D	Reprolysin	e3b2zD1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
D	KOG3538_1st	e3b2zD2	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: KOG3538_1st	ECOD (1.6)
C	Reprolysin	e3b2zC1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
C	KOG3538_1st	e3b2zC2	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: KOG3538_1st	ECOD (1.6)
B	Reprolysin	e3b2zB1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
B	KOG3538_1st	e3b2zB2	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: KOG3538_1st	ECOD (1.6)
A	Reprolysin	e3b2zA1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
A	KOG3538_1st	e3b2zA2	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: KOG3538_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
H	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
H	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)
G	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
G	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)
F	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
F	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)
E	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
E	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)
D	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
D	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)
C	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
C	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)
B	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
B	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)
A	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
A	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	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
A, B, C, D, E A, B, C, D, E, F, G, H	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	ADAMTS-4	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity metalloendopeptidase activity endopeptidase activity protein binding binding enzyme binding protease binding cation binding transition metal ion binding zinc ion binding peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity metalloendopeptidase activity endopeptidase activity protein binding binding enzyme binding protease binding cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding	developmental process multicellular organism development multicellular organismal process skeletal system development anatomical structure development system development carbohydrate derivative catabolic process glycoprotein catabolic process catabolic process carbohydrate derivative metabolic process primary metabolic process protein catabolic process glycoprotein metabolic process macromolecule catabolic process developmental process multicellular organism development multicellular organismal process skeletal system development anatomical structure development system development carbohydrate derivative catabolic process glycoprotein catabolic process catabolic process carbohydrate derivative metabolic process primary metabolic process protein catabolic process glycoprotein metabolic process macromolecule catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process proteoglycan catabolic process proteoglycan metabolic process cellular component organization extracellular matrix organization cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization cellular component disassembly extracellular matrix disassembly defense response to bacterium biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to bacterium response to stress response to external stimulus response to external biotic stimulus response to biotic stimulus proteolysis	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membraneless organelle intracellular membrane-bounded organelle intracellular organelle lumen nuclear speck ribonucleoprotein granule intracellular organelle nuclear body cellular anatomical structure nucleoplasm organelle lumen membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membraneless organelle intracellular membrane-bounded organelle intracellular organelle lumen nuclear speck ribonucleoprotein granule intracellular organelle nuclear body cellular anatomical structure nucleoplasm organelle lumen organelle membraneless organelle supramolecular complex nuclear ribonucleoprotein granule nuclear lumen cell periphery extracellular matrix external encapsulating structure extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR013273	ADAMTS/ADAMTS-like	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR001590	Peptidase M12B, ADAM/reprolysin	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR000884	Thrombospondin type-1 (TSP1) repeat	Repeat
A, B, C, D, E A, B, C, D, E, F, G, H	IPR041645	ADAMTS, cysteine-rich domain 2	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR010294	ADAMTS/ADAMTS-like, Spacer 1	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR045371	ADAMTS/ADAMTS-like, cysteine-rich domain 3	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036383	Thrombospondin type-1 repeat superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR006586	ADAM, cysteine-rich domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR050439	ADAMTS and ADAMTS-like	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H	Pharos: O75173	allergic rhinitis intervertebral disc degenerative disorder psoriasis breast cancer osteoarthritis congestive heart failure osteosarcoma

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.