Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KRY

Crystal structure of MMP-13 in complex with SC-78080

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 1998

Chain	Residue
A	HIS172
A	ASP174
A	HIS187
A	HIS200

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1999

Chain	Residue
A	HIS222
A	HIS226
A	HIS232
A	3KR1800

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1996

Chain	Residue
A	ASP162
A	ASN194
A	GLY196
A	ASP198
A	HOH303
A	HOH14

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1997

Chain	Residue
A	ASP179
A	GLY180
A	SER182
A	LEU184
A	ASP202
A	GLU205

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 3KR A 1800

Chain	Residue
A	HOH33
A	LEU184
A	LEU185
A	ALA186
A	VAL219
A	HIS222
A	GLU223
A	HIS226
A	HIS232
A	ALA238
A	LEU239
A	PHE241
A	PRO242
A	ILE243
A	TYR244
A	THR245
A	HOH299
A	HOH328
A	ZN1999

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 2998

Chain	Residue
B	HIS172
B	ASP174
B	HIS187
B	HIS200

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 2999

Chain	Residue
B	HIS222
B	HIS226
B	HIS232
B	3KR2800

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 2996

Chain	Residue
B	HOH96
B	ASP162
B	ASN194
B	GLY196
B	ASP198
B	HOH295

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 2997

Chain	Residue
B	ASP179
B	GLY180
B	SER182
B	LEU184
B	ASP202
B	GLU205

site_id	BC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 3KR B 2800

Chain	Residue
B	LEU184
B	LEU185
B	ALA186
B	LEU218
B	VAL219
B	HIS222
B	GLU223
B	HIS226
B	HIS232
B	ALA238
B	LEU239
B	PHE241
B	PRO242
B	ILE243
B	TYR244
B	THR245
B	THR247
B	HOH302
B	HOH419
B	HOH519
B	ZN2999

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 3998

Chain	Residue
C	HIS172
C	ASP174
C	HIS187
C	HIS200

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 3999

Chain	Residue
C	HIS222
C	HIS226
C	HIS232
C	3KR3800

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 3996

Chain	Residue
C	ASP162
C	ASN194
C	GLY196
C	ASP198
C	HOH283
C	HOH438

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 3997

Chain	Residue
C	GLU205
C	ASP179
C	GLY180
C	SER182
C	LEU184
C	ASP202

site_id	BC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 3KR C 3800

Chain	Residue
C	GLY183
C	LEU184
C	LEU185
C	ALA186
C	LEU218
C	VAL219
C	HIS222
C	GLU223
C	HIS226
C	HIS232
C	LEU239
C	PHE241
C	PRO242
C	ILE243
C	TYR244
C	THR245
C	THR247
C	HOH368
C	HOH483
C	ZN3999

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 4998

Chain	Residue
D	HIS172
D	ASP174
D	HIS187
D	HIS200

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 4999

Chain	Residue
D	HIS222
D	HIS226
D	HIS232
D	3KR4800

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 4996

Chain	Residue
D	ASP162
D	ASN194
D	GLY196
D	ASP198
D	HOH286
D	HOH305

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 4997

Chain	Residue
D	ASP179
D	GLY180
D	SER182
D	LEU184
D	ASP202
D	GLU205

site_id	CC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 3KR D 4800

Chain	Residue
D	GLY183
D	LEU184
D	LEU185
D	ALA186
D	LEU218
D	VAL219
D	HIS222
D	GLU223
D	HIS226
D	HIS232
D	LEU239
D	PHE241
D	PRO242
D	ILE243
D	TYR244
D	THR245
D	THR247
D	ZN4999

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL219-LEU228

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000305\|PubMed:23913860

Chain	Residue	Details
A	GLU223
B	GLU223
C	GLU223
D	GLU223

site_id	SWS_FT_FI2
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:10926524, ECO:0000269\|PubMed:10986126, ECO:0000269\|PubMed:15734645, ECO:0000269\|PubMed:15780611, ECO:0000269\|PubMed:17196980, ECO:0000269\|PubMed:17623656, ECO:0000269\|PubMed:19422229, ECO:0000269\|PubMed:20005097, ECO:0000269\|PubMed:20726512, ECO:0000269\|PubMed:22689580, ECO:0000269\|PubMed:23810497, ECO:0000269\|PubMed:23913860, ECO:0000269\|PubMed:8969305

Chain	Residue	Details
A	ASP128
A	ASP202
A	ASP203
A	GLU205
B	ASP128
B	ASP162
B	ASP179
B	GLY180
B	SER182
B	LEU184
B	ASN194
A	ASP162
B	GLY196
B	ASP198
B	ASP202
B	ASP203
B	GLU205
C	ASP128
C	ASP162
C	ASP179
C	GLY180
C	SER182
A	ASP179
C	LEU184
C	ASN194
C	GLY196
C	ASP198
C	ASP202
C	ASP203
C	GLU205
D	ASP128
D	ASP162
D	ASP179
A	GLY180
D	GLY180
D	SER182
D	LEU184
D	ASN194
D	GLY196
D	ASP198
D	ASP202
D	ASP203
D	GLU205
A	SER182
A	LEU184
A	ASN194
A	GLY196
A	ASP198

site_id	SWS_FT_FI3
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269\|PubMed:10926524, ECO:0000269\|PubMed:10986126, ECO:0000269\|PubMed:15734645, ECO:0000269\|PubMed:15780611, ECO:0000269\|PubMed:17196980, ECO:0000269\|PubMed:17623656, ECO:0000269\|PubMed:19422229, ECO:0000269\|PubMed:20005097, ECO:0000269\|PubMed:20726512, ECO:0000269\|PubMed:22689580, ECO:0000269\|PubMed:23810497, ECO:0000269\|PubMed:23913860

Chain	Residue	Details
A	HIS172
B	ASP174
B	HIS187
B	HIS200
B	HIS222
B	HIS226
B	HIS232
B	MET240
C	HIS172
C	ASP174
C	HIS187
A	ASP174
C	HIS200
C	HIS222
C	HIS226
C	HIS232
C	MET240
D	HIS172
D	ASP174
D	HIS187
D	HIS200
D	HIS222
A	HIS187
D	HIS226
D	HIS232
D	MET240
A	HIS200
A	HIS222
A	HIS226
A	HIS232
A	MET240
B	HIS172

site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:8576151

Chain	Residue	Details
A	ASN117
B	ASN117
C	ASN117
D	ASN117

site_id	SWS_FT_FI5
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN152
B	ASN152
C	ASN152
D	ASN152

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