5JMO
X-ray structure of furin in complex with the inhibitory antibody Nb14
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH |
| Chain | Residue | Details |
| A | VAL149-HIS160 |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA |
| Chain | Residue | Details |
| A | HIS194-ALA204 |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG |
| Chain | Residue | Details |
| A | GLY366-GLY376 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 |
| Chain | Residue | Details |
| A | ASP153 | |
| A | HIS194 | |
| A | SER368 | |
| B | ASP153 | |
| B | HIS194 | |
| B | SER368 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD |
| Chain | Residue | Details |
| A | ASP115 | |
| A | ASP258 | |
| A | ASP301 | |
| A | GLU331 | |
| B | ASP115 | |
| B | ASP162 | |
| B | ASP174 | |
| B | ASP179 | |
| B | ASP181 | |
| B | VAL205 | |
| B | ASN208 | |
| A | ASP162 | |
| B | VAL210 | |
| B | GLY212 | |
| B | ASP258 | |
| B | ASP301 | |
| B | GLU331 | |
| A | ASP174 | |
| A | ASP179 | |
| A | ASP181 | |
| A | VAL205 | |
| A | ASN208 | |
| A | VAL210 | |
| A | GLY212 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD |
| Chain | Residue | Details |
| A | ASP154 | |
| B | ASP154 | |
| B | ASP191 | |
| B | GLU236 | |
| B | SER253 | |
| B | ASP264 | |
| B | ALA292 | |
| B | ASP306 | |
| B | TYR308 | |
| B | SER368 | |
| A | ASP191 | |
| A | GLU236 | |
| A | SER253 | |
| A | ASP264 | |
| A | ALA292 | |
| A | ASP306 | |
| A | TYR308 | |
| A | SER368 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN387 | |
| A | ASN440 | |
| A | ASN553 | |
| B | ASN387 | |
| B | ASN440 | |
| B | ASN553 |
