eF-site ID 1suv-ABCDEF PDB Code 1suv Chain A, B, C, D, E, F click to enlarge Title Structure of Human Transferrin Receptor-Transferrin Complex Classification METAL TRANSPORT Compound Transferrin receptor protein 1 Source Homo sapiens (Human) (1SUV) Sequence A:  LYWDDLKRKLSEKLDSTDFTSTIKLLNENSYVPREAGSQK DENLALYVENEFREFKLSKVWRDQHFVKIQVKDSAQNSVI IVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKK DFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLI YMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQF PPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDS TCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDH YVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDG FQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTY INLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQF LYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDT DYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKL THDVELNLDYEEYNSQLLSFVRDLNQYRADIKEMGLSLQW LYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRV EYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQ NNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF B:  LYWDDLKRKLSEKLDSTDFTSTIKLLNENSYVPREAGSQK DENLALYVENEFREFKLSKVWRDQHFVKIQVKDSAQNSVI IVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKK DFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLI YMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQF PPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDS TCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDH YVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDG FQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTY INLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQF LYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDT DYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKL THDVELNLDYEEYNSQLLSFVRDLNQYRADIKEMGLSLQW LYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRV EYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQ NNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF C:  DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKK ASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVA EFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGL GRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCA DGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDV AFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCH LAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEF QLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTA IRNLREGTC D:  DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKK ASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVA EFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGL GRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCA DGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDV AFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCH LAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEF QLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTA IRNLREGTC E:  PDPLQDECKAVKWCALGHHERLKCDEWSVTSGGLIECESA ETPEDCIAKIMNGEADAMSLDGGYVYIAGQCGLVPVLAEN YESTDCKKAPEEGYLSVAVVKKSNPDINWNNLEGKKSCHT AVDRTAGWNIPMGLLYNRINHCRFDEFFRQGCAPGSQKNS SLCELCVGPSVCAPNNREGYYGYTGAFRCLVEKGDVAFVK SQTVLQNTGGRNSEPWAKDLKEEDFELLCLDGTRKPVSEA HNCHLAKAPNHAVVSRKDKAACVKQKLLDLQVEFGNTVAD CSSKFCMFHSKTKDLLFRDDTKCLVDLRGKNTYEKYLGAD YIKAVSNLRKCSTSRLLEACTFHKH F:  PDPLQDECKAVKWCALGHHERLKCDEWSVTSGGLIECESA ETPEDCIAKIMNGEADAMSLDGGYVYIAGQCGLVPVLAEN YESTDCKKAPEEGYLSVAVVKKSNPDINWNNLEGKKSCHT AVDRTAGWNIPMGLLYNRINHCRFDEFFRQGCAPGSQKNS SLCELCVGPSVCAPNNREGYYGYTGAFRCLVEKGDVAFVK SQTVLQNTGGRNSEPWAKDLKEEDFELLCLDGTRKPVSEA HNCHLAKAPNHAVVSRKDKAACVKQKLLDLQVEFGNTVAD CSSKFCMFHSKTKDLLFRDDTKCLVDLRGKNTYEKYLGAD YIKAVSNLRKCSTSRLLEACTFHKH Description (1)  Transferrin receptor protein 1, Serotransferrin Functional site 1) chain C residue 63 type sequence D description BINDING SITE FOR RESIDUE CO3 C 338 source : AC1 2) chain C residue 95 type sequence Y description BINDING SITE FOR RESIDUE CO3 C 338 source : AC1 3) chain C residue 120 type sequence T description BINDING SITE FOR RESIDUE CO3 C 338 source : AC1 4) chain C residue 124 type sequence R description BINDING SITE FOR RESIDUE CO3 C 338 source : AC1 5) chain C residue 126 type sequence A description BINDING SITE FOR RESIDUE CO3 C 338 source : AC1 6) chain C residue 127 type sequence G description BINDING SITE FOR RESIDUE CO3 C 338 source : AC1 7) chain C residue 188 type sequence Y description BINDING SITE FOR RESIDUE CO3 C 338 source : AC1 8) chain C residue 249 type sequence H description BINDING SITE FOR RESIDUE CO3 C 338 source : AC1 9) chain C residue 63 type sequence D description BINDING SITE FOR RESIDUE FE C 339 source : AC2 10) chain C residue 95 type sequence Y description BINDING SITE FOR RESIDUE FE C 339 source : AC2 11) chain C residue 188 type sequence Y description BINDING SITE FOR RESIDUE FE C 339 source : AC2 12) chain C residue 249 type sequence H description BINDING SITE FOR RESIDUE FE C 339 source : AC2 13) chain D residue 63 type sequence D description BINDING SITE FOR RESIDUE CO3 D 338 source : AC3 14) chain D residue 95 type sequence Y description BINDING SITE FOR RESIDUE CO3 D 338 source : AC3 15) chain D residue 120 type sequence T description BINDING SITE FOR RESIDUE CO3 D 338 source : AC3 16) chain D residue 124 type sequence R description BINDING SITE FOR RESIDUE CO3 D 338 source : AC3 17) chain D residue 126 type sequence A description BINDING SITE FOR RESIDUE CO3 D 338 source : AC3 18) chain D residue 127 type sequence G description BINDING SITE FOR RESIDUE CO3 D 338 source : AC3 19) chain D residue 188 type sequence Y description BINDING SITE FOR RESIDUE CO3 D 338 source : AC3 20) chain D residue 249 type sequence H description BINDING SITE FOR RESIDUE CO3 D 338 source : AC3 21) chain D residue 63 type sequence D description BINDING SITE FOR RESIDUE FE D 339 source : AC4 22) chain D residue 95 type sequence Y description BINDING SITE FOR RESIDUE FE D 339 source : AC4 23) chain D residue 188 type sequence Y description BINDING SITE FOR RESIDUE FE D 339 source : AC4 24) chain D residue 249 type sequence H description BINDING SITE FOR RESIDUE FE D 339 source : AC4 25) chain E residue 392 type sequence D description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 26) chain E residue 425 type sequence Y description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 27) chain E residue 451 type sequence T description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 28) chain E residue 455 type sequence R description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 29) chain E residue 456 type sequence T description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 30) chain E residue 457 type sequence A description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 31) chain E residue 458 type sequence G description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 32) chain E residue 514 type sequence Y description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 33) chain E residue 582 type sequence H description BINDING SITE FOR RESIDUE CO3 E 701 source : AC5 34) chain E residue 392 type sequence D description BINDING SITE FOR RESIDUE FE E 703 source : AC6 35) chain E residue 425 type sequence Y description BINDING SITE FOR RESIDUE FE E 703 source : AC6 36) chain E residue 514 type sequence Y description BINDING SITE FOR RESIDUE FE E 703 source : AC6 37) chain E residue 582 type sequence H description BINDING SITE FOR RESIDUE FE E 703 source : AC6 38) chain F residue 392 type sequence D description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 39) chain F residue 425 type sequence Y description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 40) chain F residue 451 type sequence T description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 41) chain F residue 455 type sequence R description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 42) chain F residue 456 type sequence T description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 43) chain F residue 457 type sequence A description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 44) chain F residue 458 type sequence G description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 45) chain F residue 514 type sequence Y description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 46) chain F residue 582 type sequence H description BINDING SITE FOR RESIDUE CO3 F 701 source : AC7 47) chain F residue 392 type sequence D description BINDING SITE FOR RESIDUE FE F 703 source : AC8 48) chain F residue 425 type sequence Y description BINDING SITE FOR RESIDUE FE F 703 source : AC8 49) chain F residue 514 type sequence Y description BINDING SITE FOR RESIDUE FE F 703 source : AC8 50) chain F residue 582 type sequence H description BINDING SITE FOR RESIDUE FE F 703 source : AC8 51) chain C residue 63 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 52) chain C residue 95 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 53) chain C residue 188 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 54) chain C residue 249 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 55) chain D residue 63 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 56) chain D residue 95 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 57) chain D residue 188 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 58) chain D residue 249 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 59) chain C residue 120 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 60) chain C residue 124 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 61) chain C residue 126 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 62) chain C residue 127 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 63) chain D residue 120 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 64) chain D residue 124 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 65) chain D residue 126 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 66) chain D residue 127 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 67) chain C residue 23 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:P12346 source Swiss-Prot : SWS_FT_FI3 68) chain D residue 23 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:P12346 source Swiss-Prot : SWS_FT_FI3 69) chain C residue 32 type CARBOHYD sequence S description O-linked (GalNAc...) serine source Swiss-Prot : SWS_FT_FI4 70) chain D residue 32 type CARBOHYD sequence S description O-linked (GalNAc...) serine source Swiss-Prot : SWS_FT_FI4 71) chain C residue 95-104 type prosite sequence YYAVAVVKKD description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD source prosite : PS00205 72) chain E residue 425-434 type prosite sequence YLSVAVVKKS description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD source prosite : PS00205 73) chain C residue 188-204 type prosite sequence YSGAFKCLKDGAGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF source prosite : PS00206 74) chain E residue 514-529 type prosite sequence YTGAFRCLVEKGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF source prosite : PS00206 75) chain C residue 222-252 type prosite sequence QYELLCLDNTRKPVDEYKDCHLAQVPSHTVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV source prosite : PS00207 76) chain E residue 555-585 type prosite sequence DFELLCLDGTRKPVSEAHNCHLAKAPNHAVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV source prosite : PS00207

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