Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6ELA

Crystal structure of MMP12 in complex with inhibitor BE4.

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
C	0004222	molecular_function	metalloendopeptidase activity
C	0006508	biological_process	proteolysis
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0031012	cellular_component	extracellular matrix
D	0004222	molecular_function	metalloendopeptidase activity
D	0006508	biological_process	proteolysis
D	0008237	molecular_function	metallopeptidase activity
D	0008270	molecular_function	zinc ion binding
D	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	HIS218
A	HIS222
A	HIS228
A	B9Z306

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

Chain	Residue
A	HIS168
A	ASP170
A	HIS183
A	HIS196

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 303

Chain	Residue
A	GLY190
A	GLY192
A	ASP194
A	HOH411
A	HOH453
A	ASP158

site_id	AC4
Number of Residues	5
Details	binding site for residue CA A 304

Chain	Residue
A	ASP124
A	GLU199
A	GLU201
A	HOH535
A	HOH548

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

Chain	Residue
A	ASP175
A	GLY176
A	GLY178
A	ILE180
A	ASP198
A	GLU201

site_id	AC6
Number of Residues	18
Details	binding site for residue B9Z A 306

Chain	Residue
A	GLY179
A	ALA182
A	HIS218
A	GLU219
A	HIS222
A	HIS228
A	VAL235
A	PHE237
A	PRO238
A	THR239
A	TYR240
A	ZN301
A	DIO307
A	HOH408
A	HOH424
A	HOH437
A	HOH449
A	HOH514

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

Chain	Residue
A	ALA184
A	B9Z306
A	HOH414

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS218
B	HIS222
B	HIS228
B	B9Z306

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN B 302

Chain	Residue
B	HIS168
B	ASP170
B	HIS183
B	HIS196

site_id	AD1
Number of Residues	6
Details	binding site for residue CA B 303

Chain	Residue
B	ASP158
B	GLY190
B	GLY192
B	ASP194
B	HOH428
B	HOH467

site_id	AD2
Number of Residues	5
Details	binding site for residue CA B 304

Chain	Residue
B	ASP124
B	GLU199
B	GLU201
B	HOH525
B	HOH534

site_id	AD3
Number of Residues	6
Details	binding site for residue CA B 305

Chain	Residue
B	ASP175
B	GLY176
B	GLY178
B	ILE180
B	ASP198
B	GLU201

site_id	AD4
Number of Residues	15
Details	binding site for residue B9Z B 306

Chain	Residue
B	ALA182
B	HIS218
B	GLU219
B	HIS222
B	HIS228
B	VAL235
B	PHE237
B	PRO238
B	THR239
B	TYR240
B	ZN301
B	DIO307
B	HOH436
B	HOH450
B	HOH512

site_id	AD5
Number of Residues	5
Details	binding site for residue DIO B 307

Chain	Residue
B	HIS172
B	HIS183
B	ALA184
B	PHE185
B	B9Z306

site_id	AD6
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS218
C	HIS222
C	HIS228
C	B9Z307

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN C 302

Chain	Residue
C	HIS168
C	ASP170
C	HIS183
C	HIS196

site_id	AD8
Number of Residues	6
Details	binding site for residue CA C 303

Chain	Residue
C	ASP158
C	GLY190
C	GLY192
C	ASP194
C	HOH422
C	HOH489

site_id	AD9
Number of Residues	5
Details	binding site for residue CA C 304

Chain	Residue
C	ASP124
C	GLU199
C	GLU201
C	HOH525
C	HOH549

site_id	AE1
Number of Residues	6
Details	binding site for residue CA C 305

Chain	Residue
C	ASP175
C	GLY176
C	GLY178
C	ILE180
C	ASP198
C	GLU201

site_id	AE2
Number of Residues	2
Details	binding site for residue EDO C 306

Chain	Residue
C	ASN246
C	HOH424

site_id	AE3
Number of Residues	18
Details	binding site for residue B9Z C 307

Chain	Residue
C	GLY179
C	ALA182
C	HIS218
C	GLU219
C	HIS222
C	HIS228
C	VAL235
C	PHE237
C	PRO238
C	THR239
C	TYR240
C	ZN301
C	DIO308
C	HOH423
C	HOH435
C	HOH450
C	HOH455
C	HOH502

site_id	AE4
Number of Residues	3
Details	binding site for residue DIO C 308

Chain	Residue
C	ALA184
C	PHE185
C	B9Z307

site_id	AE5
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS218
D	HIS222
D	HIS228
D	B9Z306

site_id	AE6
Number of Residues	4
Details	binding site for residue ZN D 302

Chain	Residue
D	HIS168
D	ASP170
D	HIS183
D	HIS196

site_id	AE7
Number of Residues	6
Details	binding site for residue CA D 303

Chain	Residue
D	ASP158
D	GLY190
D	GLY192
D	ASP194
D	HOH406
D	HOH450

site_id	AE8
Number of Residues	5
Details	binding site for residue CA D 304

Chain	Residue
D	ASP124
D	GLU199
D	GLU201
D	HOH538
D	HOH551

site_id	AE9
Number of Residues	6
Details	binding site for residue CA D 305

Chain	Residue
D	ASP175
D	GLY176
D	GLY178
D	ILE180
D	ASP198
D	GLU201

site_id	AF1
Number of Residues	16
Details	binding site for residue B9Z D 306

Chain	Residue
D	ALA182
D	THR215
D	HIS218
D	GLU219
D	HIS222
D	HIS228
D	VAL235
D	PHE237
D	PRO238
D	THR239
D	TYR240
D	ZN301
D	DIO307
D	DIO308
D	HOH428
D	HOH445

site_id	AF2
Number of Residues	3
Details	binding site for residue DIO D 307

Chain	Residue
D	ILE180
D	B9Z306
D	HOH545

site_id	AF3
Number of Residues	3
Details	binding site for residue DIO D 308

Chain	Residue
D	HIS172
D	ALA184
D	B9Z306

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR215-LEU224

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	76
Details	Binding site: {}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)