eF-site ID 6hzb-A PDB Code 6hzb Chain A click to enlarge Title X-ray structure of furin in complex with the cyclic inhibitor c[glutaryl-Arg-Arg-Lys]-Lys-4-Amba Classification HYDROLASE Compound Furin Source (6HZB) Sequence A:  VYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIV VSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQ MNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLD GEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPAR LAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGY TNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNE KQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNL TWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGL LDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVR KTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSP MGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWV LEIENTSEANNYGTLTKFTLVLYGTASGSLVPR Description Functional site 1) chain A residue 174 type sequence D description binding site for residue CA A 601 source : AC1 2) chain A residue 179 type sequence D description binding site for residue CA A 601 source : AC1 3) chain A residue 181 type sequence D description binding site for residue CA A 601 source : AC1 4) chain A residue 115 type sequence D description binding site for residue CA A 602 source : AC2 5) chain A residue 162 type sequence D description binding site for residue CA A 602 source : AC2 6) chain A residue 205 type sequence V description binding site for residue CA A 602 source : AC2 7) chain A residue 208 type sequence N description binding site for residue CA A 602 source : AC2 8) chain A residue 210 type sequence V description binding site for residue CA A 602 source : AC2 9) chain A residue 212 type sequence G description binding site for residue CA A 602 source : AC2 10) chain A residue 258 type sequence D description binding site for residue CA A 603 source : AC3 11) chain A residue 301 type sequence D description binding site for residue CA A 603 source : AC3 12) chain A residue 331 type sequence E description binding site for residue CA A 603 source : AC3 13) chain A residue 309 type sequence T description binding site for residue NA A 604 source : AC4 14) chain A residue 311 type sequence S description binding site for residue NA A 604 source : AC4 15) chain A residue 314 type sequence T description binding site for residue NA A 604 source : AC4 16) chain A residue 279 type sequence S description binding site for residue NA A 605 source : AC5 17) chain A residue 284 type sequence G description binding site for residue NA A 605 source : AC5 18) chain A residue 544 type sequence S description binding site for residue NA A 606 source : AC6 19) chain A residue 544 type sequence S description binding site for residue NA A 606 source : AC6 20) chain A residue 276 type sequence R description binding site for residue CL A 607 source : AC7 21) chain A residue 449 type sequence K description binding site for residue CL A 607 source : AC7 22) chain A residue 571 type sequence Y description binding site for residue CL A 607 source : AC7 23) chain A residue 118 type sequence F description binding site for residue PO4 A 608 source : AC8 24) chain A residue 119 type sequence P description binding site for residue PO4 A 608 source : AC8 25) chain A residue 121 type sequence Q description binding site for residue PO4 A 608 source : AC8 26) chain A residue 125 type sequence S description binding site for residue PO4 A 608 source : AC8 27) chain A residue 326 type sequence V description binding site for residue PO4 A 609 source : AC9 28) chain A residue 346 type sequence Q description binding site for residue PO4 A 609 source : AC9 29) chain A residue 347 type sequence N description binding site for residue PO4 A 609 source : AC9 30) chain A residue 408 type sequence A description binding site for residue PO4 A 609 source : AC9 31) chain A residue 409 type sequence N description binding site for residue PO4 A 609 source : AC9 32) chain A residue 263 type sequence V description binding site for residue DMS A 610 source : AD1 33) chain A residue 527 type sequence G description binding site for residue DMS A 610 source : AD1 34) chain A residue 528 type sequence F description binding site for residue DMS A 610 source : AD1 35) chain A residue 529 type sequence N description binding site for residue DMS A 610 source : AD1 36) chain A residue 257 type sequence E description binding site for residue PTD B 101 source : AD2 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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 43) 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 44) 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 45) 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 46) chain A residue 440 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 47) chain A residue 553 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 48) chain A residue 387 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 49) chain A residue 149-160 type prosite sequence VSILDDGIEKNH description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH source prosite : PS00136 50) chain A residue 194-204 type prosite sequence HGTRCAGEVAA description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA source prosite : PS00137 51) chain A residue 366-376 type prosite sequence GTSASAPLAAG description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG source prosite : PS00138 52) chain A residue 153 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 194 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 368 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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

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