4XCT

Crystal structure of a hydroxamate based inhibitor ARP101 (EN73) in complex with the MMP-9 catalytic domain.

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	16
Details	binding site for residue N73 A 301

Chain	Residue
A	LEU187
A	TYR245
A	PRO246
A	MET247
A	TYR248
A	ZN302
A	PGO315
A	HOH501
A	LEU188
A	ALA189
A	LEU222
A	HIS226
A	GLU227
A	HIS230
A	HIS236
A	LEU243

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 302

Chain	Residue
A	HIS226
A	HIS230
A	HIS236
A	N73301

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 303

Chain	Residue
A	HIS175
A	ASP177
A	HIS190
A	HIS203

---

site_id	AC4
Number of Residues	6
Details	binding site for residue CA A 304

Chain	Residue
A	ASP182
A	GLY183
A	ASP185
A	LEU187
A	ASP205
A	GLU208

---

site_id	AC5
Number of Residues	6
Details	binding site for residue CA A 305

Chain	Residue
A	ASP165
A	GLY197
A	GLN199
A	ASP201
A	HOH415
A	HOH452

---

site_id	AC6
Number of Residues	5
Details	binding site for residue CA A 306

Chain	Residue
A	ASP131
A	ASP206
A	GLU208
A	HOH512
A	HOH515

---

site_id	AC7
Number of Residues	3
Details	binding site for residue DMS A 307

Chain	Residue
A	HIS190
A	ALA191
A	PHE192

---

site_id	AC8
Number of Residues	2
Details	binding site for residue DMS A 308

Chain	Residue
A	THR157
A	ASP182

---

site_id	AC9
Number of Residues	6
Details	binding site for residue EDO A 309

Chain	Residue
A	ILE125
A	GLN126
A	TYR128
A	ALA173
A	GLU174
A	HOH460

---

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO A 310

Chain	Residue
A	SER211
A	LEU212
A	GLY215
A	VAL216
A	HIS266
A	HOH495

---

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO A 311

Chain	Residue
A	HIS118
A	HIS119
A	ASN120
A	HOH407

---

site_id	AD3
Number of Residues	2
Details	binding site for residue EDO A 312

Chain	Residue
A	LEU187
A	ASN262

---

site_id	AD4
Number of Residues	8
Details	binding site for residue GOL A 313

Chain	Residue
A	ASP113
A	LYS115
A	TRP116
A	HIS117
A	HIS118
A	GLY195
A	HOH406
A	HOH436

---

site_id	AD5
Number of Residues	5
Details	binding site for residue PGO A 314

Chain	Residue
A	ARG162
A	GLY183
A	LYS184
A	ASP207
A	HOH537

---

site_id	AD6
Number of Residues	5
Details	binding site for residue PGO A 315

Chain	Residue
A	PRO240
A	ALA242
A	ARG249
A	N73301
A	HOH429

---

site_id	AD7
Number of Residues	4
Details	binding site for residue BUD A 316

Chain	Residue
A	HIS117
A	GLU130
A	LEU132
A	PRO133

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---