Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OZR

MMP13 Catalytic Domain Complexed with 4-{[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl}benzoic acid

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
E	0004222	molecular_function	metalloendopeptidase activity
E	0006508	biological_process	proteolysis
E	0008237	molecular_function	metallopeptidase activity
E	0008270	molecular_function	zinc ion binding
E	0031012	cellular_component	extracellular matrix
F	0004222	molecular_function	metalloendopeptidase activity
F	0006508	biological_process	proteolysis
F	0008237	molecular_function	metallopeptidase activity
F	0008270	molecular_function	zinc ion binding
F	0031012	cellular_component	extracellular matrix
G	0004222	molecular_function	metalloendopeptidase activity
G	0006508	biological_process	proteolysis
G	0008237	molecular_function	metallopeptidase activity
G	0008270	molecular_function	zinc ion binding
G	0031012	cellular_component	extracellular matrix
H	0004222	molecular_function	metalloendopeptidase activity
H	0006508	biological_process	proteolysis
H	0008237	molecular_function	metallopeptidase activity
H	0008270	molecular_function	zinc ion binding
H	0031012	cellular_component	extracellular matrix

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	VAL198-LEU207

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	560
Details	Region: {"description":"Interaction with TIMP2"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"evidences":[{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	96
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10926524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10986126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15734645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17623656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19422229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20005097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20726512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22689580","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23810497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8969305","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	64
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10926524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10986126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15734645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17623656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19422229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20005097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20726512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22689580","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23810497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8576151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
A	MET219
A	GLU202

site_id	CSA10
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
B	GLU202

site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
C	GLU202

site_id	CSA12
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
D	GLU202

site_id	CSA13
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
E	GLU202

site_id	CSA14
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
F	GLU202

site_id	CSA15
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
G	GLU202

site_id	CSA16
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
H	GLU202

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
B	MET219
B	GLU202

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
C	MET219
C	GLU202

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
D	MET219
D	GLU202

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
E	MET219
E	GLU202

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
F	MET219
F	GLU202

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
G	MET219
G	GLU202

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
H	MET219
H	GLU202

site_id	CSA9
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
A	GLU202

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