8K5Y

Crystal structure of human proMMP-9 catalytic domain in complex with inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0031012	cellular_component	extracellular matrix
B	0004222	molecular_function	metalloendopeptidase activity
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0031012	cellular_component	extracellular matrix

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHAL

Chain	Residue	Details
A	VAL223-LEU232

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

Chain	Residue	Details
A	PRO97-LEU104

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:12051944

Chain	Residue	Details
A	GLU227
B	GLU227

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: in inhibited form => ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439

Chain	Residue	Details
A	CYS99
B	CYS99

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site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:12051944

Chain	Residue	Details
A	ASP131
A	ASP205
A	ASP206
A	GLU208
B	ASP131
B	ASP165
B	ASP182
B	GLY183
B	ASP185
B	LEU187
B	GLY197
A	ASP165
B	GLN199
B	ASP201
B	ASP205
B	ASP206
B	GLU208
A	ASP182
A	GLY183
A	ASP185
A	LEU187
A	GLY197
A	GLN199
A	ASP201

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site_id	SWS_FT_FI4
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439

Chain	Residue	Details
A	HIS175
B	HIS190
B	HIS203
B	HIS226
B	HIS230
B	HIS236
A	ASP177
A	HIS190
A	HIS203
A	HIS226
A	HIS230
A	HIS236
B	HIS175
B	ASP177

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site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Cleavage; by MMP3 => ECO:0000269|PubMed:1371271

Chain	Residue	Details
A	GLU59
A	ARG106
B	GLU59
B	ARG106

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site_id	SWS_FT_FI6
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN38
A	ASN120
A	ASN127
B	ASN38
B	ASN120
B	ASN127

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