4H3X

Crystal structure of an MMP broad spectrum hydroxamate based inhibitor CC27 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
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 PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS226
A	HIS230
A	HIS236
A	10B306

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 302

Chain	Residue
A	HIS175
A	ASP177
A	HIS190
A	HIS203

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 303

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

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 304

Chain	Residue
A	ASP131
A	ASP206
A	GLU208
A	HOH452
A	HOH453

---

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	HOH406
A	HOH411

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 10B A 306

Chain	Residue
A	GLY186
A	LEU187
A	LEU188
A	ALA189
A	LEU222
A	HIS226
A	GLU227
A	HIS230
A	HIS236
A	LEU243
A	TYR245
A	MET247
A	ZN301
A	HOH415
A	HOH492
B	TYR245
B	PRO246

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 307

Chain	Residue
A	PRO254
A	HOH421
B	PRO254
B	PRO255
B	HOH448
B	HOH451

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 308

Chain	Residue
A	ASP177
A	GLY178
A	GOL311
A	HOH476
A	HOH515
A	HOH553
A	HOH559
A	HOH560
A	HOH590

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 309

Chain	Residue
A	TYR179
A	LEU187
A	HIS190
A	HOH594
A	HOH595
B	PRO240
B	TYR245

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PGO A 310

Chain	Residue
A	ALA173
A	GLU174

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 311

Chain	Residue
A	GOL308
A	HOH480
A	HOH515
A	HOH529
A	HOH553

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 312

Chain	Residue
A	ASN120
A	THR122
A	THR157
A	HOH536

---

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 313

Chain	Residue
A	HOH434
A	HOH483

---

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS226
B	HIS230
B	HIS236
B	10B306

---

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 302

Chain	Residue
B	HIS175
B	ASP177
B	HIS190
B	HIS203

---

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 303

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

---

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 304

Chain	Residue
B	ASP131
B	ASP206
B	GLU208
B	HOH468
B	HOH529

---

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 305

Chain	Residue
B	ASP201
B	HOH401
B	HOH405
B	ASP165
B	GLY197
B	GLN199

---

site_id	CC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 10B B 306

Chain	Residue
A	TYR245
A	PRO246
A	MET247
B	GLY186
B	LEU187
B	LEU188
B	ALA189
B	LEU222
B	HIS226
B	GLU227
B	HIS230
B	HIS236
B	LEU243
B	TYR245
B	MET247
B	TYR248
B	ZN301
B	HOH444

---

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 307

Chain	Residue
B	PHE250
B	THR251
B	HOH423
B	HOH515
B	HOH546

---

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG B 308

Chain	Residue
B	PEG309
B	HOH442
B	HOH443
B	HOH480

---

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 309

Chain	Residue
B	TYR179
B	PEG308
B	HOH442

---

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	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	14
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	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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