eF-site ID 4omd-D PDB Code 4omd Chain D 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 D:  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 D residue 276 type sequence R description BINDING SITE FOR RESIDUE FMT C 602 source : BC5 2) chain D residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT D 601 source : CC1 3) chain D residue 447 type sequence Q description BINDING SITE FOR RESIDUE FMT D 601 source : CC1 4) chain D residue 275 type sequence F description BINDING SITE FOR RESIDUE FMT D 602 source : CC2 5) chain D residue 313 type sequence Y description BINDING SITE FOR RESIDUE FMT D 602 source : CC2 6) chain D residue 449 type sequence K description BINDING SITE FOR RESIDUE FMT D 602 source : CC2 7) chain D residue 571 type sequence Y description BINDING SITE FOR RESIDUE FMT D 602 source : CC2 8) chain D residue 115 type sequence D description BINDING SITE FOR RESIDUE CA D 603 source : CC3 9) chain D residue 162 type sequence D description BINDING SITE FOR RESIDUE CA D 603 source : CC3 10) chain D residue 205 type sequence V description BINDING SITE FOR RESIDUE CA D 603 source : CC3 11) chain D residue 208 type sequence N description BINDING SITE FOR RESIDUE CA D 603 source : CC3 12) chain D residue 210 type sequence V description BINDING SITE FOR RESIDUE CA D 603 source : CC3 13) chain D residue 212 type sequence G description BINDING SITE FOR RESIDUE CA D 603 source : CC3 14) chain D residue 258 type sequence D description BINDING SITE FOR RESIDUE CA D 604 source : CC4 15) chain D residue 301 type sequence D description BINDING SITE FOR RESIDUE CA D 604 source : CC4 16) chain D residue 331 type sequence E description BINDING SITE FOR RESIDUE CA D 604 source : CC4 17) chain D residue 174 type sequence D description BINDING SITE FOR RESIDUE CA D 605 source : CC5 18) chain D residue 179 type sequence D description BINDING SITE FOR RESIDUE CA D 605 source : CC5 19) chain D residue 181 type sequence D description BINDING SITE FOR RESIDUE CA D 605 source : CC5 20) chain D residue 309 type sequence T description BINDING SITE FOR RESIDUE NA D 606 source : CC6 21) chain D residue 311 type sequence S description BINDING SITE FOR RESIDUE NA D 606 source : CC6 22) chain D residue 314 type sequence T description BINDING SITE FOR RESIDUE NA D 606 source : CC6 23) chain D residue 154 type sequence D description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 24) chain D residue 191 type sequence D description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 25) chain D residue 192 type sequence N description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 26) chain D residue 194 type sequence H description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 27) chain D residue 231 type sequence V description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 28) chain D residue 236 type sequence E description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 29) chain D residue 253 type sequence S description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 30) chain D residue 254 type sequence W description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 31) chain D residue 255 type sequence G description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 32) chain D residue 256 type sequence P description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 33) chain D residue 258 type sequence D description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 34) chain D residue 264 type sequence D description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 35) chain D residue 265 type sequence G description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 36) chain D residue 292 type sequence A description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 37) chain D residue 295 type sequence N description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 38) chain D residue 306 type sequence D description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 39) chain D residue 308 type sequence Y description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 40) chain D residue 309 type sequence T description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 41) chain D residue 367 type sequence T description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 42) chain D residue 368 type sequence S description BINDING SITE FOR CHAIN K OF PHENYLACETYL-ARG-VAL-ARG-(AMIDOMETHYL)BENZAMIDINE source : EC4 43) chain D residue 153 type ACT_SITE sequence D description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 44) chain D residue 194 type ACT_SITE sequence H description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 45) chain D residue 368 type ACT_SITE sequence S description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 source Swiss-Prot : SWS_FT_FI1 46) chain D 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 47) chain D 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 48) chain D 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 49) chain D 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 50) chain D 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 51) chain D 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 52) chain D 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 53) chain D 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 54) chain D 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 55) chain D 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 D 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 D 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 D 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 59) chain D 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 60) chain D 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 61) chain D 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 62) chain D 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 63) chain D 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 64) chain D 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 65) chain D 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 66) chain D 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 67) chain D residue 387 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 68) chain D residue 440 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 69) chain D residue 553 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI4

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