eF-site ID 4omd-A PDB Code 4omd Chain A click to enlarge Title X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba Classification HYDROLASE/HYDROLASE INHIBITOR Compound Furin Source Homo sapiens (Human) (4OMD) Sequence A:  VYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIV VSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQ MNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLD GEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPAR LAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGY TNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNE KQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNL TWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGL LDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVR KTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSP MGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWV LEIENTSEANNYGTLTKFTLVLYGTA Description (1)  Furin (E.C.3.4.21.75), phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine Functional site 1) chain A residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT A 601 source : AC1 2) chain A residue 447 type sequence Q description BINDING SITE FOR RESIDUE FMT A 601 source : AC1 3) chain A residue 275 type sequence F description BINDING SITE FOR RESIDUE FMT A 602 source : AC2 4) chain A residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT A 602 source : AC2 5) chain A residue 449 type sequence K description BINDING SITE FOR RESIDUE FMT A 602 source : AC2 6) chain A residue 571 type sequence Y description BINDING SITE FOR RESIDUE FMT A 602 source : AC2 7) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE CA A 603 source : AC3 8) chain A residue 162 type sequence D description BINDING SITE FOR RESIDUE CA A 603 source : AC3 9) chain A residue 205 type sequence V description BINDING SITE FOR RESIDUE CA A 603 source : AC3 10) chain A residue 208 type sequence N description BINDING SITE FOR RESIDUE CA A 603 source : AC3 11) chain A residue 210 type sequence V description BINDING SITE FOR RESIDUE CA A 603 source : AC3 12) chain A residue 212 type sequence G description BINDING SITE FOR RESIDUE CA A 603 source : AC3 13) chain A residue 258 type sequence D description BINDING SITE FOR RESIDUE CA A 604 source : AC4 14) chain A residue 301 type sequence D description BINDING SITE FOR RESIDUE CA A 604 source : AC4 15) chain A residue 331 type sequence E description BINDING SITE FOR RESIDUE CA A 604 source : AC4 16) chain A residue 174 type sequence D description BINDING SITE FOR RESIDUE CA A 605 source : AC5 17) chain A residue 179 type sequence D description BINDING SITE FOR RESIDUE CA A 605 source : AC5 18) chain A residue 181 type sequence D description BINDING SITE FOR RESIDUE CA A 605 source : AC5 19) chain A residue 309 type sequence T description BINDING SITE FOR RESIDUE NA A 606 source : AC6 20) chain A residue 311 type sequence S description BINDING SITE FOR RESIDUE NA A 606 source : AC6 21) chain A residue 314 type sequence T description BINDING SITE FOR RESIDUE NA A 606 source : AC6 22) chain A residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT B 601 source : AC7 23) chain A residue 280 type sequence Q description BINDING SITE FOR RESIDUE FMT B 601 source : AC7 24) chain A residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT B 602 source : AC8 25) chain A residue 154 type sequence D description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 26) chain A residue 191 type sequence D description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 27) chain A residue 192 type sequence N description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 28) chain A residue 194 type sequence H description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 29) chain A residue 231 type sequence V description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 30) chain A residue 236 type sequence E description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 31) chain A residue 253 type sequence S description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 32) chain A residue 254 type sequence W description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 33) chain A residue 255 type sequence G description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 34) chain A residue 256 type sequence P description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 35) chain A residue 258 type sequence D description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 36) chain A residue 264 type sequence D description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 37) chain A residue 265 type sequence G description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 38) chain A residue 292 type sequence A description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 39) chain A residue 293 type sequence S description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 40) chain A residue 295 type sequence N description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 41) chain A residue 306 type sequence D description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 42) chain A residue 308 type sequence Y description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 43) chain A residue 367 type sequence T description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 44) chain A residue 368 type sequence S description BINDING SITE FOR CHAIN H OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC1 45) chain A residue 153 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 194 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 47) chain A residue 368 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 48) 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 49) 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 50) 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 51) 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 52) 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 53) 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 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) chain A residue 387 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 70) chain A residue 440 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 71) chain A residue 553 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 72) chain A residue 149-160 type prosite sequence VSILDDGIEKNH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH source prosite : PS00136 73) chain A residue 194-204 type prosite sequence HGTRCAGEVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA source prosite : PS00137 74) chain A residue 366-376 type prosite sequence GTSASAPLAAG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG source prosite : PS00138

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