eF-site ID 4omc-E PDB Code 4omc Chain E 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 E:  YQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVV SILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQM NDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDG EVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARL AEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYT NSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEK QIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLT WRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLL DAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRK TVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPM GTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVL EIENTSEANNYGTLTKFTLVLYGTA Description (1)  Furin (E.C.3.4.21.75), meta-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine Functional site 1) chain E residue 298 type sequence R description BINDING SITE FOR RESIDUE FMT A 601 source : AC1 2) chain E residue 365 type sequence T description BINDING SITE FOR RESIDUE FMT E 601 source : DC6 3) chain E residue 527 type sequence G description BINDING SITE FOR RESIDUE FMT E 602 source : DC7 4) chain E residue 528 type sequence F description BINDING SITE FOR RESIDUE FMT E 602 source : DC7 5) chain E residue 529 type sequence N description BINDING SITE FOR RESIDUE FMT E 602 source : DC7 6) chain E residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT E 603 source : DC8 7) chain E residue 447 type sequence Q description BINDING SITE FOR RESIDUE FMT E 603 source : DC8 8) chain E residue 275 type sequence F description BINDING SITE FOR RESIDUE FMT E 604 source : DC9 9) chain E residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT E 604 source : DC9 10) chain E residue 449 type sequence K description BINDING SITE FOR RESIDUE FMT E 604 source : DC9 11) chain E residue 571 type sequence Y description BINDING SITE FOR RESIDUE FMT E 604 source : DC9 12) chain E residue 115 type sequence D description BINDING SITE FOR RESIDUE CA E 605 source : EC1 13) chain E residue 162 type sequence D description BINDING SITE FOR RESIDUE CA E 605 source : EC1 14) chain E residue 205 type sequence V description BINDING SITE FOR RESIDUE CA E 605 source : EC1 15) chain E residue 208 type sequence N description BINDING SITE FOR RESIDUE CA E 605 source : EC1 16) chain E residue 210 type sequence V description BINDING SITE FOR RESIDUE CA E 605 source : EC1 17) chain E residue 212 type sequence G description BINDING SITE FOR RESIDUE CA E 605 source : EC1 18) chain E residue 258 type sequence D description BINDING SITE FOR RESIDUE CA E 606 source : EC2 19) chain E residue 301 type sequence D description BINDING SITE FOR RESIDUE CA E 606 source : EC2 20) chain E residue 331 type sequence E description BINDING SITE FOR RESIDUE CA E 606 source : EC2 21) chain E residue 174 type sequence D description BINDING SITE FOR RESIDUE CA E 607 source : EC3 22) chain E residue 179 type sequence D description BINDING SITE FOR RESIDUE CA E 607 source : EC3 23) chain E residue 181 type sequence D description BINDING SITE FOR RESIDUE CA E 607 source : EC3 24) chain E residue 309 type sequence T description BINDING SITE FOR RESIDUE NA E 608 source : EC4 25) chain E residue 311 type sequence S description BINDING SITE FOR RESIDUE NA E 608 source : EC4 26) chain E residue 314 type sequence T description BINDING SITE FOR RESIDUE NA E 608 source : EC4 27) chain E residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT F 601 source : EC5 28) chain E residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT F 602 source : EC6 29) chain E residue 154 type sequence D description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 30) chain E residue 191 type sequence D description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 31) chain E residue 192 type sequence N description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 32) chain E residue 194 type sequence H description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 33) chain E residue 231 type sequence V description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 34) chain E residue 232 type sequence T description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 35) chain E residue 236 type sequence E description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 36) chain E residue 253 type sequence S description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 37) chain E residue 254 type sequence W description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 38) chain E residue 255 type sequence G description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 39) chain E residue 256 type sequence P description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 40) chain E residue 258 type sequence D description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 41) chain E residue 264 type sequence D description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 42) chain E residue 265 type sequence G description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 43) chain E residue 292 type sequence A description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 44) chain E residue 295 type sequence N description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 45) chain E residue 306 type sequence D description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 46) chain E residue 308 type sequence Y description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 47) chain E residue 367 type sequence T description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 48) chain E residue 368 type sequence S description BINDING SITE FOR CHAIN L OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC8 49) chain E residue 153 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 50) chain E residue 194 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 51) chain E residue 368 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 52) chain E 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 53) chain E 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 54) chain E 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 55) chain E 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 56) chain E 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 57) chain E 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 58) chain E 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 59) chain E 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 60) chain E 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 61) chain E 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 62) chain E 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 63) chain E 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 64) chain E 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 65) chain E 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 66) chain E 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 67) chain E 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 68) chain E 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 69) chain E 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 70) chain E 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 71) chain E 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 72) chain E 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 73) chain E residue 387 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 74) chain E residue 440 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 75) chain E residue 553 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4

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