eF-site ID 4omc-B PDB Code 4omc Chain B 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 B:  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 B residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT A 603 source : AC3 2) chain B residue 280 type sequence Q description BINDING SITE FOR RESIDUE FMT A 603 source : AC3 3) chain B residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT A 604 source : AC4 4) chain B residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT B 601 source : AC9 5) chain B residue 447 type sequence Q description BINDING SITE FOR RESIDUE FMT B 601 source : AC9 6) chain B residue 275 type sequence F description BINDING SITE FOR RESIDUE FMT B 602 source : BC1 7) chain B residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT B 602 source : BC1 8) chain B residue 449 type sequence K description BINDING SITE FOR RESIDUE FMT B 602 source : BC1 9) chain B residue 365 type sequence T description BINDING SITE FOR RESIDUE FMT B 603 source : BC2 10) chain B residue 527 type sequence G description BINDING SITE FOR RESIDUE FMT B 604 source : BC3 11) chain B residue 528 type sequence F description BINDING SITE FOR RESIDUE FMT B 604 source : BC3 12) chain B residue 529 type sequence N description BINDING SITE FOR RESIDUE FMT B 604 source : BC3 13) chain B residue 115 type sequence D description BINDING SITE FOR RESIDUE CA B 605 source : BC4 14) chain B residue 162 type sequence D description BINDING SITE FOR RESIDUE CA B 605 source : BC4 15) chain B residue 205 type sequence V description BINDING SITE FOR RESIDUE CA B 605 source : BC4 16) chain B residue 208 type sequence N description BINDING SITE FOR RESIDUE CA B 605 source : BC4 17) chain B residue 210 type sequence V description BINDING SITE FOR RESIDUE CA B 605 source : BC4 18) chain B residue 212 type sequence G description BINDING SITE FOR RESIDUE CA B 605 source : BC4 19) chain B residue 258 type sequence D description BINDING SITE FOR RESIDUE CA B 606 source : BC5 20) chain B residue 301 type sequence D description BINDING SITE FOR RESIDUE CA B 606 source : BC5 21) chain B residue 331 type sequence E description BINDING SITE FOR RESIDUE CA B 606 source : BC5 22) chain B residue 174 type sequence D description BINDING SITE FOR RESIDUE CA B 607 source : BC6 23) chain B residue 179 type sequence D description BINDING SITE FOR RESIDUE CA B 607 source : BC6 24) chain B residue 181 type sequence D description BINDING SITE FOR RESIDUE CA B 607 source : BC6 25) chain B residue 309 type sequence T description BINDING SITE FOR RESIDUE NA B 608 source : BC7 26) chain B residue 311 type sequence S description BINDING SITE FOR RESIDUE NA B 608 source : BC7 27) chain B residue 314 type sequence T description BINDING SITE FOR RESIDUE NA B 608 source : BC7 28) chain B residue 154 type sequence D description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 29) chain B residue 191 type sequence D description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 30) chain B residue 192 type sequence N description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 31) chain B residue 194 type sequence H description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 32) chain B residue 231 type sequence V description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 33) chain B residue 232 type sequence T description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 34) chain B residue 236 type sequence E description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 35) chain B residue 253 type sequence S description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 36) chain B residue 254 type sequence W description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 37) chain B residue 255 type sequence G description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 38) chain B residue 256 type sequence P description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 39) chain B residue 258 type sequence D description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 40) chain B residue 264 type sequence D description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 41) chain B residue 265 type sequence G description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 42) chain B residue 292 type sequence A description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 43) chain B residue 306 type sequence D description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 44) chain B residue 308 type sequence Y description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 45) chain B residue 367 type sequence T description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 46) chain B residue 368 type sequence S description BINDING SITE FOR CHAIN I OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC5 47) chain B residue 153 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 194 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 368 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 50) chain B 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 51) chain B 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 52) chain B 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 53) chain B 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 54) chain B 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 55) chain B 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 56) chain B 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 57) chain B 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 58) chain B 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 59) chain B 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 60) chain B 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 61) chain B 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 62) chain B 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 63) chain B 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 64) chain B 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 65) chain B 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 66) chain B 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 67) chain B 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 68) chain B 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 69) chain B 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 70) chain B 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 71) chain B residue 387 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 72) chain B residue 440 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 73) chain B residue 553 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4

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