eF-site ID 4omc-A PDB Code 4omc Chain A 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 A:  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 A residue 295 type sequence N description BINDING SITE FOR RESIDUE FMT A 601 source : AC1 2) chain A residue 365 type sequence T description BINDING SITE FOR RESIDUE FMT A 601 source : AC1 3) chain A residue 366 type sequence G description BINDING SITE FOR RESIDUE FMT A 601 source : AC1 4) chain A residue 527 type sequence G description BINDING SITE FOR RESIDUE FMT A 602 source : AC2 5) chain A residue 529 type sequence N description BINDING SITE FOR RESIDUE FMT A 602 source : AC2 6) chain A residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT A 603 source : AC3 7) chain A residue 447 type sequence Q description BINDING SITE FOR RESIDUE FMT A 603 source : AC3 8) chain A residue 275 type sequence F description BINDING SITE FOR RESIDUE FMT A 604 source : AC4 9) chain A residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT A 604 source : AC4 10) chain A residue 449 type sequence K description BINDING SITE FOR RESIDUE FMT A 604 source : AC4 11) chain A residue 571 type sequence Y description BINDING SITE FOR RESIDUE FMT A 604 source : AC4 12) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE CA A 605 source : AC5 13) chain A residue 162 type sequence D description BINDING SITE FOR RESIDUE CA A 605 source : AC5 14) chain A residue 205 type sequence V description BINDING SITE FOR RESIDUE CA A 605 source : AC5 15) chain A residue 208 type sequence N description BINDING SITE FOR RESIDUE CA A 605 source : AC5 16) chain A residue 210 type sequence V description BINDING SITE FOR RESIDUE CA A 605 source : AC5 17) chain A residue 212 type sequence G description BINDING SITE FOR RESIDUE CA A 605 source : AC5 18) chain A residue 258 type sequence D description BINDING SITE FOR RESIDUE CA A 606 source : AC6 19) chain A residue 301 type sequence D description BINDING SITE FOR RESIDUE CA A 606 source : AC6 20) chain A residue 331 type sequence E description BINDING SITE FOR RESIDUE CA A 606 source : AC6 21) chain A residue 174 type sequence D description BINDING SITE FOR RESIDUE CA A 607 source : AC7 22) chain A residue 179 type sequence D description BINDING SITE FOR RESIDUE CA A 607 source : AC7 23) chain A residue 181 type sequence D description BINDING SITE FOR RESIDUE CA A 607 source : AC7 24) chain A residue 309 type sequence T description BINDING SITE FOR RESIDUE NA A 608 source : AC8 25) chain A residue 311 type sequence S description BINDING SITE FOR RESIDUE NA A 608 source : AC8 26) chain A residue 314 type sequence T description BINDING SITE FOR RESIDUE NA A 608 source : AC8 27) chain A residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT B 601 source : AC9 28) chain A residue 280 type sequence Q description BINDING SITE FOR RESIDUE FMT B 601 source : AC9 29) chain A residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT B 602 source : BC1 30) chain A residue 298 type sequence R description BINDING SITE FOR RESIDUE FMT E 601 source : DC6 31) chain A residue 154 type sequence D description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 32) chain A residue 191 type sequence D description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 33) chain A residue 192 type sequence N description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 34) chain A residue 194 type sequence H description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 35) chain A residue 231 type sequence V description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 36) chain A residue 232 type sequence T description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 37) chain A residue 236 type sequence E description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 38) chain A residue 253 type sequence S description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 39) chain A residue 254 type sequence W description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 40) chain A residue 255 type sequence G description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 41) chain A residue 256 type sequence P description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 42) chain A residue 258 type sequence D description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 43) chain A residue 264 type sequence D description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 44) chain A residue 265 type sequence G description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 45) chain A residue 292 type sequence A description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 46) chain A residue 306 type sequence D description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 47) chain A residue 308 type sequence Y description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 48) chain A residue 367 type sequence T description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 49) chain A residue 368 type sequence S description BINDING SITE FOR CHAIN H OF META-GUANIDINOMETHYL-PHENYLACETYL-ARG-VAL-ARG- (AMIDOMETHYL)BENZAMIDINE source : FC4 50) chain A residue 153 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 194 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 368 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 149-160 type prosite sequence VSILDDGIEKNH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH source prosite : PS00136 54) chain A residue 194-204 type prosite sequence HGTRCAGEVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA source prosite : PS00137 55) chain A residue 366-376 type prosite sequence GTSASAPLAAG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG source prosite : PS00138 56) chain A 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 57) chain A 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 58) chain A 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 59) chain A 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 60) chain A 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 61) chain A 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 62) chain A 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 63) chain A 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 64) chain A 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 65) chain A 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 66) chain A 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 67) chain A 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 68) chain A 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 69) chain A 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 70) chain A 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 71) chain A 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 72) chain A 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 73) chain A 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 74) chain A 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 75) chain A 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 76) chain A 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 77) chain A residue 387 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 78) chain A residue 440 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 79) chain A residue 553 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4

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