1FBL

STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A 993

Chain	Residue
A	ASP124
A	GLU199
A	GLU201

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 994

Chain	Residue
A	ASP285
A	GLN329
A	ASP378
A	ASP427

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 995

Chain	Residue
A	GLY192
A	ASP194
A	HOH834
A	HOH837
A	ASP158
A	GLY190

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 996

Chain	Residue
A	ASP175
A	GLY176
A	GLY178
A	ASN180
A	ASP198
A	GLU201

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 997

Chain	Residue
A	HIS168
A	ASP170
A	HIS183
A	HIS196

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 998

Chain	Residue
A	HIS218
A	HIS222
A	HIS228
A	HTA900

---

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HTA A 900

Chain	Residue
A	GLY179
A	ASN180
A	LEU181
A	ALA182
A	HIS218
A	GLU219
A	HIS222
A	HIS228
A	PRO238
A	ASN239
A	TYR240
A	HOH505
A	HOH531
A	HOH559
A	ZN998

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE317-TYR332

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

Chain	Residue	Details
A	VAL215-LEU224

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:8590015

Chain	Residue	Details
A	GLU219

---

site_id	SWS_FT_FI2
Number of Residues	23
Details	BINDING:

Chain	Residue	Details
A	HIS168
A	ASP170
A	ASP175
A	GLY176
A	GLY178
A	ASN180
A	HIS183
A	GLY190
A	GLY192
A	ASP194
A	HIS196
A	ASP198
A	GLU199
A	GLU201
A	HIS218
A	HIS222
A	HIS228
A	ASP285
A	GLN329
A	ASP378
A	ASP427
A	ASP124
A	ASP158

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Cleavage; by autolysis

Chain	Residue	Details
A	ALA258

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P03956

Chain	Residue	Details
A	THR274

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by PKDCC => ECO:0000250|UniProtKB:P03956

Chain	Residue	Details
A	TYR360

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN120

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