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 |