1USN

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THIADIAZOLE INHIBITOR PNU-142372

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	4
Details	BINDING SITE FOR RESIDUE ZN A 257

Chain	Residue
A	HIS201
A	HIS205
A	HIS211
A	IN9300

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 258

Chain	Residue
A	HIS151
A	ASP153
A	HIS166
A	HIS179

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 259

Chain	Residue
A	ASP158
A	GLY159
A	GLY161
A	VAL163
A	ASP181
A	GLU184

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 260

Chain	Residue
A	ASP141
A	GLY173
A	ASN175
A	ASP177
A	HOH307
A	HOH316

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 261

Chain	Residue
A	ASP107
A	ASP182
A	GLU184
A	HOH321
A	HOH331

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 262

Chain	Residue
A	HIS96
A	HIS96
A	HIS96
A	HOH263
A	HOH263
A	HOH263

---

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE IN9 A 300

Chain	Residue
A	TYR155
A	HIS166
A	ALA167
A	TYR168
A	ALA169
A	THR190
A	THR191
A	GLU202
A	HIS205
A	HIS211
A	ZN257
A	HOH320
A	HOH380

---

site_id	CA1
Number of Residues	6
Details	CA1 ARE THE LIGANDS OF THE CALCIUM ION CA 259.

Chain	Residue
A	ASP158
A	GLY159
A	GLY161
A	VAL163
A	ASP181
A	GLU184

---

site_id	CA2
Number of Residues	6
Details	CA2 ARE THE LIGANDS OF THE CALCIUM ION CA 260.

Chain	Residue
A	ASP141
A	GLY173
A	ASN175
A	ASP177
A	HOH306
A	HOH312

---

site_id	CA3
Number of Residues	3
Details	CA3 ARE THE LIGANDS OF THE CALCIUM ION CA 261.

Chain	Residue
A	ASP107
A	ASP182
A	GLU184

---

site_id	INH
Number of Residues	8
Details	SITE INH IS THE BINDING SITE FOR THE UREA-THIADIAZOLE INHIBITOR PNU-142372; IN9 300.

Chain	Residue
A	PHE86
A	TYR155
A	HIS166
A	ALA167
A	TYR168
A	ALA169
A	HIS205
A	PHE210

---

site_id	ZN1
Number of Residues	4
Details	ZN1 ARE THE LIGANDS OF THE CATALYTIC (ZN 257) ZINC ION.

Chain	Residue
A	HIS205
A	HIS211
A	IN9300
A	HIS201

---

site_id	ZN2
Number of Residues	4
Details	ZN2 ARE THE LIGANDS OF THE STRUCTURAL (ZN 258) ZINC ION.

Chain	Residue
A	HIS151
A	ASP153
A	HIS166
A	HIS179

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL198-LEU207

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8740360","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
A	MET219
A	GLU202

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
A	GLU202

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 591

Chain	Residue	Details
A	HIS201	metal ligand
A	GLU202	proton acceptor, proton donor
A	HIS205	metal ligand
A	HIS211	metal ligand

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