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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | DPS502 |
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 | 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 | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | PRO109 |
A | PRO109 |
A | LYS110 |
A | LYS110 |
A | HOH542 |
A | HOH542 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 304 |
Chain | Residue |
A | ASP141 |
A | GLY173 |
A | ASN175 |
A | ASP177 |
A | HOH574 |
A | HOH575 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 305 |
Chain | Residue |
A | ASP107 |
A | ASP182 |
A | GLU184 |
A | HOH576 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE DPS A 502 |
Chain | Residue |
A | LEU164 |
A | ALA165 |
A | ALA167 |
A | HIS201 |
A | GLU202 |
A | HIS205 |
A | PHE210 |
A | HIS211 |
A | TYR220 |
A | PRO221 |
A | LEU222 |
A | TYR223 |
A | HIS224 |
A | ZN301 |
A | HOH566 |
site_id | CA1 |
Number of Residues | 1 |
Details | CA1 IS THE FIRST CALCIUM BINDING SITE. |
site_id | CA2 |
Number of Residues | 1 |
Details | CA2 IS THE SECOND CALCIUM BINDING SITE. |
site_id | CA3 |
Number of Residues | 1 |
Details | CA3 IS THE THIRD CALCIUM BINDING SITE. |
site_id | IN2 |
Number of Residues | 1 |
Details | IN2 IS THE BINDING SITE FOR THE DIPHENYLPIPERIDINE SULFONAMIDE INHIBITOR. |
site_id | ZN1 |
Number of Residues | 1 |
Details | ZN1 IS THE CATALYTIC ZINC BINDING SITE. |
site_id | ZN2 |
Number of Residues | 1 |
Details | ZN1 IS THE STRUCTURAL ZINC BINDING SITE. |
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 | 1 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | GLU202 | |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP107 | |
A | GLY173 | |
A | ASN175 | |
A | ASP177 | |
A | HIS179 | |
A | ASP181 | |
A | ASP182 | |
A | GLU184 | |
A | ASP141 | |
A | HIS151 | |
A | ASP153 | |
A | ASP158 | |
A | GLY159 | |
A | GLY161 | |
A | VAL163 | |
A | HIS166 | |
Chain | Residue | Details |
A | HIS201 | |
A | HIS205 | |
A | HIS211 | |
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 | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1hfs |
Chain | Residue | Details |
A | GLU202 | |
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 |