eF-site ID 4omc-C PDB Code 4omc Chain C click to enlarge Title X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba Classification HYDROLASE/HYDROLASE INHIBITOR Compound Furin Source Homo sapiens (Human) (4OMC) Sequence C:  VYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIV VSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQ MNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLD GEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPAR LAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGY TNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNE KQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNL TWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGL LDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVR KTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSP MGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWV LEIENTSEANNYGTLTKFTLVLYGTA Description (1)  Furin (E.C.3.4.21.75), meta-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine Functional site 1) chain C residue 295 type sequence N description BINDING SITE FOR RESIDUE FMT C 601 source : BC8 2) chain C residue 365 type sequence T description BINDING SITE FOR RESIDUE FMT C 601 source : BC8 3) chain C residue 366 type sequence G description BINDING SITE FOR RESIDUE FMT C 601 source : BC8 4) chain C residue 527 type sequence G description BINDING SITE FOR RESIDUE FMT C 602 source : BC9 5) chain C residue 529 type sequence N description BINDING SITE FOR RESIDUE FMT C 602 source : BC9 6) chain C residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT C 603 source : CC1 7) chain C residue 447 type sequence Q description BINDING SITE FOR RESIDUE FMT C 603 source : CC1 8) chain C residue 275 type sequence F description BINDING SITE FOR RESIDUE FMT C 604 source : CC2 9) chain C residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT C 604 source : CC2 10) chain C residue 449 type sequence K description BINDING SITE FOR RESIDUE FMT C 604 source : CC2 11) chain C residue 571 type sequence Y description BINDING SITE FOR RESIDUE FMT C 604 source : CC2 12) chain C residue 115 type sequence D description BINDING SITE FOR RESIDUE CA C 605 source : CC3 13) chain C residue 162 type sequence D description BINDING SITE FOR RESIDUE CA C 605 source : CC3 14) chain C residue 205 type sequence V description BINDING SITE FOR RESIDUE CA C 605 source : CC3 15) chain C residue 208 type sequence N description BINDING SITE FOR RESIDUE CA C 605 source : CC3 16) chain C residue 210 type sequence V description BINDING SITE FOR RESIDUE CA C 605 source : CC3 17) chain C residue 212 type sequence G description BINDING SITE FOR RESIDUE CA C 605 source : CC3 18) chain C residue 258 type sequence D description BINDING SITE FOR RESIDUE CA C 606 source : CC4 19) chain C residue 301 type sequence D description BINDING SITE FOR RESIDUE CA C 606 source : CC4 20) chain C residue 331 type sequence E description BINDING SITE FOR RESIDUE CA C 606 source : CC4 21) chain C residue 174 type sequence D description BINDING SITE FOR RESIDUE CA C 607 source : CC5 22) chain C residue 179 type sequence D description BINDING SITE FOR RESIDUE CA C 607 source : CC5 23) chain C residue 181 type sequence D description BINDING SITE FOR RESIDUE CA C 607 source : CC5 24) chain C residue 309 type sequence T description BINDING SITE FOR RESIDUE NA C 608 source : CC6 25) chain C residue 311 type sequence S description BINDING SITE FOR RESIDUE NA C 608 source : CC6 26) chain C residue 314 type sequence T description BINDING SITE FOR RESIDUE NA C 608 source : CC6 27) chain C residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT D 601 source : CC7 28) chain C residue 280 type sequence Q description BINDING SITE FOR RESIDUE FMT D 601 source : CC7 29) chain C residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT D 602 source : CC8 30) chain C residue 298 type sequence R description BINDING SITE FOR RESIDUE FMT F 603 source : EC7 31) chain C residue 154 type sequence D description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 32) chain C residue 191 type sequence D description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 33) chain C residue 192 type sequence N description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 34) chain C residue 194 type sequence H description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 35) chain C residue 231 type sequence V description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 36) chain C residue 232 type sequence T description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 37) chain C residue 236 type sequence E description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 38) chain C residue 253 type sequence S description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 39) chain C residue 254 type sequence W description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 40) chain C residue 255 type sequence G description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 41) chain C residue 256 type sequence P description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 42) chain C residue 258 type sequence D description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 43) chain C residue 264 type sequence D description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 44) chain C residue 265 type sequence G description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 45) chain C residue 292 type sequence A description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 46) chain C residue 293 type sequence S description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 47) chain C residue 306 type sequence D description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 48) chain C residue 308 type sequence Y description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 49) chain C residue 367 type sequence T description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 50) chain C residue 368 type sequence S description BINDING SITE FOR CHAIN J OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC6 51) chain C residue 153 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 52) chain C residue 194 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 53) chain C residue 368 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 54) chain C residue 115 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 55) chain C residue 162 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 56) chain C residue 174 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 57) chain C residue 179 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 58) chain C residue 181 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 59) chain C residue 205 type BINDING sequence V description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 60) chain C residue 208 type BINDING sequence N description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 61) chain C residue 210 type BINDING sequence V description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 62) chain C residue 212 type BINDING sequence G description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 63) chain C residue 258 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 64) chain C residue 301 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 65) chain C residue 331 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI2 66) chain C residue 154 type BINDING sequence D description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 67) chain C residue 191 type BINDING sequence D description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 68) chain C residue 236 type BINDING sequence E description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 69) chain C residue 253 type BINDING sequence S description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 70) chain C residue 264 type BINDING sequence D description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 71) chain C residue 292 type BINDING sequence A description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 72) chain C residue 306 type BINDING sequence D description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 73) chain C residue 308 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 74) chain C residue 368 type BINDING sequence S description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD source Swiss-Prot : SWS_FT_FI3 75) chain C residue 387 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 76) chain C residue 440 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 77) chain C residue 553 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4

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