4OMD
X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba
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 |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0008236 | molecular_function | serine-type peptidase activity |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| F | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 601 |
| Chain | Residue |
| A | TYR313 |
| A | GLN447 |
| A | FMT602 |
| B | GLN280 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 602 |
| Chain | Residue |
| B | ARG276 |
| A | PHE275 |
| A | TYR313 |
| A | LYS449 |
| A | TYR571 |
| A | FMT601 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 603 |
| Chain | Residue |
| A | ASP115 |
| A | ASP162 |
| A | VAL205 |
| A | ASN208 |
| A | VAL210 |
| A | GLY212 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 604 |
| Chain | Residue |
| A | ASP258 |
| A | ASP301 |
| A | GLU331 |
| A | HOH746 |
| A | HOH758 |
| A | HOH796 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 605 |
| Chain | Residue |
| A | ASP174 |
| A | ASP179 |
| A | ASP181 |
| A | HOH723 |
| A | HOH727 |
| A | HOH809 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 606 |
| Chain | Residue |
| A | THR309 |
| A | SER311 |
| A | THR314 |
| A | HOH764 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 601 |
| Chain | Residue |
| A | ARG276 |
| A | GLN280 |
| B | TYR313 |
| B | GLN447 |
| B | FMT602 |
| B | HOH742 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 602 |
| Chain | Residue |
| A | ARG276 |
| B | PHE275 |
| B | TYR313 |
| B | LYS449 |
| B | TYR571 |
| B | FMT601 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 603 |
| Chain | Residue |
| B | ASP115 |
| B | ASP162 |
| B | VAL205 |
| B | ASN208 |
| B | VAL210 |
| B | GLY212 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 604 |
| Chain | Residue |
| B | ASP258 |
| B | ASP301 |
| B | GLU331 |
| B | HOH711 |
| B | HOH735 |
| B | HOH782 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 605 |
| Chain | Residue |
| B | ASP174 |
| B | ASP179 |
| B | ASP181 |
| B | HOH769 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 606 |
| Chain | Residue |
| B | THR309 |
| B | SER311 |
| B | THR314 |
| B | SER316 |
| B | HOH703 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT C 601 |
| Chain | Residue |
| C | TYR313 |
| C | GLN447 |
| C | FMT602 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT C 602 |
| Chain | Residue |
| C | PHE275 |
| C | TYR313 |
| C | LYS449 |
| C | TYR571 |
| C | FMT601 |
| D | ARG276 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 603 |
| Chain | Residue |
| C | ASP115 |
| C | ASP162 |
| C | VAL205 |
| C | ASN208 |
| C | VAL210 |
| C | GLY212 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 604 |
| Chain | Residue |
| C | ASP258 |
| C | ASP301 |
| C | GLU331 |
| C | HOH725 |
| C | HOH742 |
| C | HOH769 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 605 |
| Chain | Residue |
| C | ASP174 |
| C | ASP179 |
| C | ASP181 |
| C | HOH773 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 606 |
| Chain | Residue |
| C | THR309 |
| C | SER311 |
| C | THR314 |
| C | HOH718 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT D 601 |
| Chain | Residue |
| D | HOH760 |
| C | ARG276 |
| C | GLN280 |
| D | TYR313 |
| D | GLN447 |
| D | FMT602 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT D 602 |
| Chain | Residue |
| C | ARG276 |
| D | PHE275 |
| D | TYR313 |
| D | LYS449 |
| D | TYR571 |
| D | FMT601 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 603 |
| Chain | Residue |
| D | ASP115 |
| D | ASP162 |
| D | VAL205 |
| D | ASN208 |
| D | VAL210 |
| D | GLY212 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 604 |
| Chain | Residue |
| D | ASP258 |
| D | ASP301 |
| D | GLU331 |
| D | HOH710 |
| D | HOH725 |
| D | HOH797 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 605 |
| Chain | Residue |
| D | ASP174 |
| D | ASP179 |
| D | ASP181 |
| D | HOH749 |
| D | HOH798 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 606 |
| Chain | Residue |
| D | THR309 |
| D | SER311 |
| D | THR314 |
| D | HOH721 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT E 601 |
| Chain | Residue |
| E | TYR313 |
| E | GLN447 |
| E | FMT602 |
| E | HOH740 |
| F | ARG276 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT E 602 |
| Chain | Residue |
| E | PHE275 |
| E | TYR313 |
| E | LYS449 |
| E | TYR571 |
| E | FMT601 |
| F | ARG276 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 603 |
| Chain | Residue |
| E | ASP115 |
| E | ASP162 |
| E | VAL205 |
| E | ASN208 |
| E | VAL210 |
| E | GLY212 |
| site_id | DC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 604 |
| Chain | Residue |
| E | ASP258 |
| E | ASP301 |
| E | GLU331 |
| E | HOH718 |
| E | HOH719 |
| E | HOH788 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA E 605 |
| Chain | Residue |
| E | ASP174 |
| E | ASP179 |
| E | ASP181 |
| E | HOH789 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA E 606 |
| Chain | Residue |
| E | THR309 |
| E | SER311 |
| E | THR314 |
| E | HOH704 |
| site_id | DC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT F 601 |
| Chain | Residue |
| E | ARG276 |
| F | TYR313 |
| F | GLN447 |
| F | FMT602 |
| site_id | DC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT F 602 |
| Chain | Residue |
| E | ARG276 |
| F | PHE275 |
| F | TYR313 |
| F | LYS449 |
| F | TYR571 |
| F | FMT601 |
| site_id | DC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA F 603 |
| Chain | Residue |
| F | ASP115 |
| F | ASP162 |
| F | VAL205 |
| F | ASN208 |
| F | VAL210 |
| F | GLY212 |
| site_id | DC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA F 604 |
| Chain | Residue |
| F | ASP258 |
| F | ASP301 |
| F | GLU331 |
| F | HOH704 |
| site_id | DC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA F 605 |
| Chain | Residue |
| F | ASP174 |
| F | ASP179 |
| F | ASP181 |
| F | HOH739 |
| F | HOH757 |
| F | HOH776 |
| site_id | DC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA F 606 |
| Chain | Residue |
| F | THR309 |
| F | SER311 |
| F | THR314 |
| F | HOH715 |
| site_id | EC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE |
| Chain | Residue |
| A | ASP154 |
| A | ASP191 |
| A | ASN192 |
| A | HIS194 |
| A | VAL231 |
| A | GLU236 |
| A | SER253 |
| A | TRP254 |
| A | GLY255 |
| A | PRO256 |
| A | ASP258 |
| A | ASP264 |
| A | GLY265 |
| A | ALA292 |
| A | SER293 |
| A | ASN295 |
| A | ASP306 |
| A | TYR308 |
| A | THR367 |
| A | SER368 |
| H | HOH101 |
| H | HOH102 |
| site_id | EC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR CHAIN I OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE |
| Chain | Residue |
| B | ASP154 |
| B | ASP191 |
| B | ASN192 |
| B | HIS194 |
| B | VAL231 |
| B | GLU236 |
| B | SER253 |
| B | TRP254 |
| B | GLY255 |
| B | PRO256 |
| B | ASP258 |
| B | ASP264 |
| B | GLY265 |
| B | ALA292 |
| B | SER293 |
| B | GLY294 |
| B | ASN295 |
| B | ASP306 |
| B | TYR308 |
| B | THR309 |
| B | THR367 |
| B | SER368 |
| I | HOH101 |
| I | HOH102 |
| site_id | EC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR CHAIN J OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE |
| Chain | Residue |
| C | ASP154 |
| C | ASP191 |
| C | ASN192 |
| C | HIS194 |
| C | VAL231 |
| C | GLU236 |
| C | SER253 |
| C | TRP254 |
| C | GLY255 |
| C | PRO256 |
| C | ASP258 |
| C | ASP264 |
| C | GLY265 |
| C | ALA292 |
| C | SER293 |
| C | ASN295 |
| C | ASP306 |
| C | TYR308 |
| C | THR309 |
| C | THR367 |
| C | SER368 |
| J | HOH101 |
| J | HOH102 |
| J | HOH103 |
| site_id | EC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE |
| Chain | Residue |
| D | ASP154 |
| D | ASP191 |
| D | ASN192 |
| D | HIS194 |
| D | VAL231 |
| D | GLU236 |
| D | SER253 |
| D | TRP254 |
| D | GLY255 |
| D | PRO256 |
| D | ASP258 |
| D | ASP264 |
| D | GLY265 |
| D | ALA292 |
| D | ASN295 |
| D | ASP306 |
| D | TYR308 |
| D | THR309 |
| D | THR367 |
| D | SER368 |
| D | HOH799 |
| K | HOH101 |
| K | HOH102 |
| site_id | EC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE |
| Chain | Residue |
| E | ASP154 |
| E | ASP191 |
| E | ASN192 |
| E | HIS194 |
| E | VAL231 |
| E | GLU236 |
| E | SER253 |
| E | TRP254 |
| E | GLY255 |
| E | PRO256 |
| E | ASP258 |
| E | ASP264 |
| E | GLY265 |
| E | ALA292 |
| E | ASN295 |
| E | ASP306 |
| E | TYR308 |
| E | THR309 |
| E | THR367 |
| E | SER368 |
| L | HOH101 |
| L | HOH102 |
| L | HOH103 |
| site_id | EC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR CHAIN N OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE |
| Chain | Residue |
| F | ASP154 |
| F | ASP191 |
| F | ASN192 |
| F | HIS194 |
| F | VAL231 |
| F | GLU236 |
| F | SER253 |
| F | TRP254 |
| F | GLY255 |
| F | PRO256 |
| F | ASP258 |
| F | ASP264 |
| F | GLY265 |
| F | ALA292 |
| F | SER293 |
| F | GLY294 |
| F | ASN295 |
| F | ASP306 |
| F | TYR308 |
| F | THR309 |
| F | THR367 |
| F | SER368 |
| F | HOH704 |
| F | HOH770 |
| N | HOH101 |
| N | HOH102 |
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 | 1884 |
| Details | Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 126 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Motif: {"description":"Cell attachment site","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24666235","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25974265","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4OMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RYD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 90 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24666235","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25974265","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4OMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RYD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 18 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






