2MZE
NMR Solution Structure of the PRO Form of Human Matrilysin (proMMP-7)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002779 | biological_process | antibacterial peptide secretion |
| A | 0002780 | biological_process | antibacterial peptide biosynthetic process |
| A | 0004175 | molecular_function | endopeptidase activity |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006508 | biological_process | proteolysis |
| A | 0006509 | biological_process | membrane protein ectodomain proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0022617 | biological_process | extracellular matrix disassembly |
| A | 0030198 | biological_process | extracellular matrix organization |
| A | 0030335 | biological_process | positive regulation of cell migration |
| A | 0030574 | biological_process | collagen catabolic process |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0031293 | biological_process | membrane protein intracellular domain proteolysis |
| A | 0042127 | biological_process | regulation of cell population proliferation |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050829 | biological_process | defense response to Gram-negative bacterium |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 301 |
| Chain | Residue |
| A | ASP133 |
| A | GLY165 |
| A | LEU166 |
| A | GLY167 |
| A | ASP169 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 302 |
| Chain | Residue |
| A | THR155 |
| A | ASP173 |
| A | GLU176 |
| A | ASP150 |
| A | GLY151 |
| A | GLY153 |
| A | ASN154 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 303 |
| Chain | Residue |
| A | HIS143 |
| A | ASP145 |
| A | HIS158 |
| A | PHE160 |
| A | HIS171 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 304 |
| Chain | Residue |
| A | CYS67 |
| A | HIS194 |
| A | HIS198 |
| A | HIS204 |
Functional Information from PROSITE/UniProt
| site_id | PS00546 |
| Number of Residues | 8 |
| Details | CYSTEINE_SWITCH Matrixins cysteine switch. PRCGvPDV |
| Chain | Residue | Details |
| A | PRO65-VAL72 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | ALA195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: in inhibited form => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS67 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 17 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP133 | |
| A | GLY167 | |
| A | ASP169 | |
| A | HIS171 | |
| A | ASP173 | |
| A | GLU176 | |
| A | HIS194 | |
| A | HIS198 | |
| A | HIS204 | |
| A | HIS143 | |
| A | ASP145 | |
| A | ASP150 | |
| A | GLY151 | |
| A | GLY153 | |
| A | THR155 | |
| A | HIS158 | |
| A | GLY165 |
