4K90
Extracellular metalloproteinase from Aspergillus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004222 | molecular_function | metalloendopeptidase activity |
A | 0005615 | cellular_component | extracellular space |
A | 0008270 | molecular_function | zinc ion binding |
B | 0004222 | molecular_function | metalloendopeptidase activity |
B | 0005615 | cellular_component | extracellular space |
B | 0008270 | molecular_function | zinc ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IVIHEYTHGL |
Chain | Residue | Details |
A | ILE426-LEU435 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90 |
Chain | Residue | Details |
B | GLU245 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90 |
Chain | Residue | Details |
A | LEU375 | |
A | ASP378 | |
A | ASP400 | |
A | ASN437 | |
A | ARG438 | |
A | THR440 | |
A | GLY442 | |
A | ASN445 | |
A | GLU459 | |
B | ASN47 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90 |
Chain | Residue | Details |
A | HIS433 | |
A | HIS429 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Important for proper folding of the protein and catalytic activity => ECO:0000305|PubMed:24100314 |
Chain | Residue | Details |
A | ARG470 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN286 |