Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CK7

GELATINASE A (FULL-LENGTH)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001525	biological_process	angiogenesis
A	0001541	biological_process	ovarian follicle development
A	0001542	biological_process	ovulation from ovarian follicle
A	0001553	biological_process	luteinization
A	0001666	biological_process	response to hypoxia
A	0001968	molecular_function	fibronectin binding
A	0004175	molecular_function	endopeptidase activity
A	0004222	molecular_function	metalloendopeptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0006979	biological_process	response to oxidative stress
A	0007162	biological_process	negative regulation of cell adhesion
A	0007507	biological_process	heart development
A	0007565	biological_process	female pregnancy
A	0007567	biological_process	parturition
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0009410	biological_process	response to xenobiotic stimulus
A	0009612	biological_process	response to mechanical stimulus
A	0014012	biological_process	peripheral nervous system axon regeneration
A	0014823	biological_process	response to activity
A	0016020	cellular_component	membrane
A	0016477	biological_process	cell migration
A	0016787	molecular_function	hydrolase activity
A	0022617	biological_process	extracellular matrix disassembly
A	0030017	cellular_component	sarcomere
A	0030163	biological_process	protein catabolic process
A	0030198	biological_process	extracellular matrix organization
A	0030335	biological_process	positive regulation of cell migration
A	0030574	biological_process	collagen catabolic process
A	0031012	cellular_component	extracellular matrix
A	0032526	biological_process	response to retinoic acid
A	0034097	biological_process	response to cytokine
A	0035094	biological_process	response to nicotine
A	0035987	biological_process	endodermal cell differentiation
A	0042542	biological_process	response to hydrogen peroxide
A	0043065	biological_process	positive regulation of apoptotic process
A	0043627	biological_process	response to estrogen
A	0045906	biological_process	negative regulation of vasoconstriction
A	0046872	molecular_function	metal ion binding
A	0048013	biological_process	ephrin receptor signaling pathway
A	0048246	biological_process	macrophage chemotaxis
A	0048771	biological_process	tissue remodeling
A	0051602	biological_process	response to electrical stimulus
A	0055093	biological_process	response to hyperoxia
A	0060740	biological_process	prostate gland epithelium morphogenesis
A	0061450	biological_process	trophoblast cell migration
A	0071345	biological_process	cellular response to cytokine stimulus
A	0071347	biological_process	cellular response to interleukin-1
A	0071392	biological_process	cellular response to estradiol stimulus
A	0071492	biological_process	cellular response to UV-A
A	0071498	biological_process	cellular response to fluid shear stress
A	1903378	biological_process	positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
A	1904645	biological_process	response to amyloid-beta
A	1904707	biological_process	positive regulation of vascular associated smooth muscle cell proliferation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 990

Chain	Residue
A	CYS102
A	HIS403
A	HIS407
A	HIS413

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 991

Chain	Residue
A	HIS178
A	ASP180
A	HIS193
A	HIS206

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 992

Chain	Residue
A	ASP185
A	GLY186
A	ASP188
A	LEU190
A	ASP208
A	GLU211

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 993

Chain	Residue
A	GLU166
A	ALA167
A	ASP168
A	GLY200
A	GLY202
A	ASP204

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 994

Chain	Residue
A	ASP476
A	ASP521
A	ASP569
A	ASP618

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 995

Chain	Residue
A	ALA522
A	VAL523
A	ALA571
A	NA996

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 996

Chain	Residue
A	ILE478
A	ALA479
A	VAL523
A	ALA571
A	VAL620
A	CL995

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 777

Chain	Residue
A	GLN52
A	TYR53
A	THR56
A	PHE57
A	ASP185
A	LEU190
A	HOH1097

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 778

Chain	Residue
A	GLN298
A	GLY299
A	THR300
A	THR307

site_id	CAA
Number of Residues	6
Details	CA 992 CATALYTIC DOMAIN

Chain	Residue
A	GLY186
A	ASP188
A	LEU190
A	ASP208
A	GLU211
A	ASP185

site_id	CAB
Number of Residues	6
Details	CA 993 CATALYTIC DOMAIN

Chain	Residue
A	GLU166
A	ALA167
A	ASP168
A	GLY200
A	GLY202
A	ASP204

site_id	CAH
Number of Residues	4
Details	CA 994 HEMOPEXIN DOMAIN

Chain	Residue
A	ASP476
A	ASP521
A	ASP569
A	ASP618

site_id	ZNA
Number of Residues	4
Details	ZN 990 ACTIVE SITE

Chain	Residue
A	CYS102
A	HIS403
A	HIS407
A	HIS413

site_id	ZNS
Number of Residues	4
Details	ZN 991 STRUCTURAL SITE

Chain	Residue
A	ASP180
A	HIS178
A	HIS193
A	HIS206

Functional Information from PROSITE/UniProt

site_id	PS00023
Number of Residues	42
Details	FN2_1 Fibronectin type-II collagen-binding domain signature. CkfPFlFngkeynsCtdtgrsdgflWCsttyNFekdgkYgFC

Chain	Residue	Details
A	CYS233-CYS274
A	CYS291-CYS332
A	CYS349-CYS390

site_id	PS00024
Number of Residues	16
Details	HEMOPEXIN Hemopexin domain signature. IAdaWnaiPdNLDAVV

Chain	Residue	Details
A	ILE606-VAL621

site_id	PS00546
Number of Residues	8
Details	CYSTEINE_SWITCH Matrixins cysteine switch. PRCGnPDV

Chain	Residue	Details
A	PRO100-VAL107

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Domain: {"description":"Fibronectin type-II 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Domain: {"description":"Fibronectin type-II 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	48
Details	Domain: {"description":"Fibronectin type-II 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	44
Details	Repeat: {"description":"Hemopexin 1"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	46
Details	Repeat: {"description":"Hemopexin 2"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	48
Details	Repeat: {"description":"Hemopexin 3"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	46
Details	Repeat: {"description":"Hemopexin 4"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	111
Details	Region: {"description":"Collagenase-like 1"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	174
Details	Region: {"description":"Collagen-binding"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	7
Details	Motif: {"description":"Cysteine switch","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Binding site: {"description":"in inhibited form","evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12032297","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GXD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12032297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GXD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12032297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GXD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8549817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RTG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 9785958, 12401069

Chain	Residue	Details
A	ALA404

site_id	MCSA1
Number of Residues	4
Details	M-CSA 906

Chain	Residue	Details
A	HIS403	metal ligand
A	ALA404	proton shuttle (general acid/base)
A	HIS407	metal ligand
A	HIS413	metal ligand

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)