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 | 18 |
Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 |
Chain | Residue | Details |
A | ASP153 | |
D | ASP153 | |
D | HIS194 | |
D | SER368 | |
E | ASP153 | |
E | HIS194 | |
E | SER368 | |
F | ASP153 | |
F | HIS194 | |
F | SER368 | |
A | HIS194 | |
A | SER368 | |
B | ASP153 | |
B | HIS194 | |
B | SER368 | |
C | ASP153 | |
C | HIS194 | |
C | SER368 |
site_id | SWS_FT_FI2 |
Number of Residues | 72 |
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 | |
C | ASP115 | |
C | ASP162 | |
C | ASP174 | |
C | ASP179 | |
C | ASP181 | |
A | ASP174 | |
C | VAL205 | |
C | ASN208 | |
C | VAL210 | |
C | GLY212 | |
C | ASP258 | |
C | ASP301 | |
C | GLU331 | |
D | ASP115 | |
D | ASP162 | |
D | ASP174 | |
A | ASP179 | |
D | ASP179 | |
D | ASP181 | |
D | VAL205 | |
D | ASN208 | |
D | VAL210 | |
D | GLY212 | |
D | ASP258 | |
D | ASP301 | |
D | GLU331 | |
E | ASP115 | |
A | ASP181 | |
E | ASP162 | |
E | ASP174 | |
E | ASP179 | |
E | ASP181 | |
E | VAL205 | |
E | ASN208 | |
E | VAL210 | |
E | GLY212 | |
E | ASP258 | |
E | ASP301 | |
A | VAL205 | |
E | GLU331 | |
F | ASP115 | |
F | ASP162 | |
F | ASP174 | |
F | ASP179 | |
F | ASP181 | |
F | VAL205 | |
F | ASN208 | |
F | VAL210 | |
F | GLY212 | |
A | ASN208 | |
F | ASP258 | |
F | ASP301 | |
F | GLU331 | |
A | VAL210 | |
A | GLY212 |
site_id | SWS_FT_FI3 |
Number of Residues | 54 |
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 | |
C | ASP154 | |
A | ASP191 | |
C | ASP191 | |
C | GLU236 | |
C | SER253 | |
C | ASP264 | |
C | ALA292 | |
C | ASP306 | |
C | TYR308 | |
C | SER368 | |
D | ASP154 | |
D | ASP191 | |
A | GLU236 | |
D | GLU236 | |
D | SER253 | |
D | ASP264 | |
D | ALA292 | |
D | ASP306 | |
D | TYR308 | |
D | SER368 | |
E | ASP154 | |
E | ASP191 | |
E | GLU236 | |
A | SER253 | |
E | SER253 | |
E | ASP264 | |
E | ALA292 | |
E | ASP306 | |
E | TYR308 | |
E | SER368 | |
F | ASP154 | |
F | ASP191 | |
F | GLU236 | |
F | SER253 | |
A | ASP264 | |
F | ASP264 | |
F | ALA292 | |
F | ASP306 | |
F | TYR308 | |
F | SER368 | |
A | ALA292 | |
A | ASP306 | |
A | TYR308 | |
A | SER368 |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN387 | |
D | ASN387 | |
D | ASN440 | |
D | ASN553 | |
E | ASN387 | |
E | ASN440 | |
E | ASN553 | |
F | ASN387 | |
F | ASN440 | |
F | ASN553 | |
A | ASN440 | |
A | ASN553 | |
B | ASN387 | |
B | ASN440 | |
B | ASN553 | |
C | ASN387 | |
C | ASN440 | |
C | ASN553 |