Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QIA

CRYSTAL STRUCTURE OF STROMELYSIN 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
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	3
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS201
A	HIS205
A	HIS211

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

Chain	Residue
A	HIS151
A	ASP153
A	HIS166
A	HIS179

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS211
B	HIS201
B	HIS205

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 302

Chain	Residue
B	HIS151
B	ASP153
B	HIS166
B	HIS179

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS201
C	HIS205
C	HIS211

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 302

Chain	Residue
C	HIS151
C	ASP153
C	HIS166
C	HIS179

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS201
D	HIS205
D	HIS211

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 302

Chain	Residue
D	HIS151
D	ASP153
D	HIS166
D	HIS179

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 303

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

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 304

Chain	Residue
A	ASP141
A	GLY173
A	ASN175
A	ASP177
A	HOH348
A	HOH374

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 305

Chain	Residue
A	ASP107
A	ASP182
A	GLU184
A	HOH382
A	HOH391

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 303

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

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 304

Chain	Residue
B	ASP141
B	GLY173
B	ASN175
B	ASP177
B	HOH1043
B	HOH1071

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 305

Chain	Residue
B	ASP107
B	ASP182
B	GLU184
B	HOH1078
B	HOH1082

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 303

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

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 304

Chain	Residue
C	ASP141
C	GLY173
C	ASN175
C	ASP177
C	HOH2077
C	HOH2078

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 305

Chain	Residue
C	ASP107
C	ASP182
C	GLU184
C	HOH2082
C	HOH2087

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 303

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

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 304

Chain	Residue
D	ASP141
D	GLY173
D	ASN175
D	ASP177
D	HOH3033
D	HOH3055

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 305

Chain	Residue
D	ASP107
D	ASP182
D	GLU184
D	HOH3062
D	HOH3066

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	4
Details	ACT_SITE:

Chain	Residue	Details
A	GLU202
B	GLU202
C	GLU202
D	GLU202

site_id	SWS_FT_FI2
Number of Residues	64
Details	BINDING:

Chain	Residue	Details
A	ASP107
A	GLY173
A	ASN175
A	ASP177
A	HIS179
A	ASP181
A	ASP182
A	GLU184
B	ASP107
B	ASP141
B	HIS151
A	ASP141
B	ASP153
B	ASP158
B	GLY159
B	GLY161
B	VAL163
B	HIS166
B	GLY173
B	ASN175
B	ASP177
B	HIS179
A	HIS151
B	ASP181
B	ASP182
B	GLU184
C	ASP107
C	ASP141
C	HIS151
C	ASP153
C	ASP158
C	GLY159
C	GLY161
A	ASP153
C	VAL163
C	HIS166
C	GLY173
C	ASN175
C	ASP177
C	HIS179
C	ASP181
C	ASP182
C	GLU184
D	ASP107
A	ASP158
D	ASP141
D	HIS151
D	ASP153
D	ASP158
D	GLY159
D	GLY161
D	VAL163
D	HIS166
D	GLY173
D	ASN175
A	GLY159
D	ASP177
D	HIS179
D	ASP181
D	ASP182
D	GLU184
A	GLY161
A	VAL163
A	HIS166

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:8740360

Chain	Residue	Details
A	HIS201
D	HIS201
D	HIS205
D	HIS211
A	HIS205
A	HIS211
B	HIS201
B	HIS205
B	HIS211
C	HIS201
C	HIS205
C	HIS211

Catalytic Information from CSA

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

site_id	MCSA2
Number of Residues	4
Details	M-CSA 591

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

site_id	MCSA3
Number of Residues	4
Details	M-CSA 591

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

site_id	MCSA4
Number of Residues	4
Details	M-CSA 591

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)