1Q3A

Crystal structure of the catalytic domain of human matrix metalloproteinase 10

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	d1q3aa_	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	Matrix metalloproteases, catalytic domain	Stromelysin-2 (MMP-10)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1q3ab_	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	Matrix metalloproteases, catalytic domain	Stromelysin-2 (MMP-10)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1q3ac_	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	Matrix metalloproteases, catalytic domain	Stromelysin-2 (MMP-10)	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	Metalloproteases (zincins), catalytic domain	8039591	3001975	SCOP2B (2022-06-29)
B	SCOP2 Family	Matrix metalloproteases, catalytic domain	8027212	4001637	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Metalloproteases (zincins), catalytic domain	8039591	3001975	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Metalloproteases (zincins), catalytic domain	8039591	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)
A	Peptidase_M10	e1q3aA1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Peptidase_M10	ECOD (1.6)
B	Peptidase_M10	e1q3aB1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Peptidase_M10	ECOD (1.6)
C	Peptidase_M10	e1q3aC1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Peptidase_M10	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	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)
C	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00413	Matrixin (Peptidase_M10)	Matrixin	The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Stromelysin-2	peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity cation binding transition metal ion binding zinc ion binding ion binding peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	collagen catabolic process catabolic process metabolic process collagen metabolic process cellular component organization extracellular matrix organization cellular process cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization cellular component disassembly extracellular matrix disassembly proteolysis primary metabolic process collagen catabolic process catabolic process metabolic process collagen metabolic process cellular component organization extracellular matrix organization cellular process cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization cellular component disassembly extracellular matrix disassembly proteolysis primary metabolic process protein metabolic process macromolecule metabolic process	extracellular region cellular anatomical entity cell periphery extracellular matrix external encapsulating structure extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR018486	Hemopexin, conserved site	Conserved Site
A, B, C	IPR021190	Peptidase M10A	Family
A, B, C	IPR002477	Peptidoglycan binding-like	Domain
A, B, C	IPR036375	Hemopexin-like domain superfamily	Homologous Superfamily
A, B, C	IPR006026	Peptidase, metallopeptidase	Domain
A, B, C	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
A, B, C	IPR018487	Hemopexin-like repeats	Repeat
A, B, C	IPR000585	Hemopexin-like domain	Domain
A, B, C	IPR021158	Peptidase M10A, cysteine switch, zinc binding site	Binding Site
A, B, C	IPR036365	PGBD-like superfamily	Homologous Superfamily
A, B, C	IPR033739	Peptidase M10A, catalytic domain	Domain
A, B, C	IPR001818	Peptidase M10, metallopeptidase	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C	Pharos: P09238	rheumatoid arthritis asthma Neoplasm Metastasis contact dermatitis peripheral arterial disease sarcoidosis chronic obstructive pulmonary disease cutaneous lupus erythematosus epilepsy head and neck cancer lung benign neoplasm psoriasis ulcerative colitis atypical teratoid rhabdoid tumor cystic fibrosis rheumatoid arthritis asthma Neoplasm Metastasis contact dermatitis peripheral arterial disease sarcoidosis chronic obstructive pulmonary disease cutaneous lupus erythematosus epilepsy head and neck cancer lung benign neoplasm psoriasis ulcerative colitis atypical teratoid rhabdoid tumor cystic fibrosis gastric cancer hereditary diffuse gastric adenocarcinoma non-small cell lung carcinoma bipolar disorder ductal breast carcinoma in situ gastric neoplasm interstitial cystitis malignant mesothelioma

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.