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 |