eF-site ID 4omd-E PDB Code 4omd Chain E 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 E:  YQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVV SILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQM NDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDG EVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARL AEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYT NSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEK QIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLT WRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLL DAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRK TVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPM GTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVL EIENTSEANNYGTLTKFTLVLYGTA Description (1)  Furin (E.C.3.4.21.75), phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine Functional site 1) chain E residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT E 601 source : CC7 2) chain E residue 447 type sequence Q description BINDING SITE FOR RESIDUE FMT E 601 source : CC7 3) chain E residue 275 type sequence F description BINDING SITE FOR RESIDUE FMT E 602 source : CC8 4) chain E residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT E 602 source : CC8 5) chain E residue 449 type sequence K description BINDING SITE FOR RESIDUE FMT E 602 source : CC8 6) chain E residue 571 type sequence Y description BINDING SITE FOR RESIDUE FMT E 602 source : CC8 7) chain E residue 115 type sequence D description BINDING SITE FOR RESIDUE CA E 603 source : CC9 8) chain E residue 162 type sequence D description BINDING SITE FOR RESIDUE CA E 603 source : CC9 9) chain E residue 205 type sequence V description BINDING SITE FOR RESIDUE CA E 603 source : CC9 10) chain E residue 208 type sequence N description BINDING SITE FOR RESIDUE CA E 603 source : CC9 11) chain E residue 210 type sequence V description BINDING SITE FOR RESIDUE CA E 603 source : CC9 12) chain E residue 212 type sequence G description BINDING SITE FOR RESIDUE CA E 603 source : CC9 13) chain E residue 258 type sequence D description BINDING SITE FOR RESIDUE CA E 604 source : DC1 14) chain E residue 301 type sequence D description BINDING SITE FOR RESIDUE CA E 604 source : DC1 15) chain E residue 331 type sequence E description BINDING SITE FOR RESIDUE CA E 604 source : DC1 16) chain E residue 174 type sequence D description BINDING SITE FOR RESIDUE CA E 605 source : DC2 17) chain E residue 179 type sequence D description BINDING SITE FOR RESIDUE CA E 605 source : DC2 18) chain E residue 181 type sequence D description BINDING SITE FOR RESIDUE CA E 605 source : DC2 19) chain E residue 309 type sequence T description BINDING SITE FOR RESIDUE NA E 606 source : DC3 20) chain E residue 311 type sequence S description BINDING SITE FOR RESIDUE NA E 606 source : DC3 21) chain E residue 314 type sequence T description BINDING SITE FOR RESIDUE NA E 606 source : DC3 22) chain E residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT F 601 source : DC4 23) chain E residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT F 602 source : DC5 24) chain E residue 154 type sequence D description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 25) chain E residue 191 type sequence D description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 26) chain E residue 192 type sequence N description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 27) chain E residue 194 type sequence H description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 28) chain E residue 231 type sequence V description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 29) chain E residue 236 type sequence E description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 30) chain E residue 253 type sequence S description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 31) chain E residue 254 type sequence W description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 32) chain E residue 255 type sequence G description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 33) chain E residue 256 type sequence P description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 34) chain E residue 258 type sequence D description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 35) chain E residue 264 type sequence D description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 36) chain E residue 265 type sequence G description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 37) chain E residue 292 type sequence A description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 38) chain E residue 295 type sequence N description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 39) chain E residue 306 type sequence D description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 40) chain E residue 308 type sequence Y description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 41) chain E residue 309 type sequence T description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 42) chain E residue 367 type sequence T description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 43) chain E residue 368 type sequence S description BINDING SITE FOR CHAIN L OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC5 44) chain E residue 153 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 45) chain E residue 194 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 46) chain E residue 368 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 47) 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 48) 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 49) 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 50) 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 51) 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 52) 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 53) 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 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) chain E residue 387 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 69) chain E residue 440 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 70) 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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