eF-site ID 1suv-C PDB Code 1suv Chain C 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 C:  DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKK ASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVA EFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGL GRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCA DGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDV AFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCH LAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEF QLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTA IRNLREGTC 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 C residue 95-104 type prosite sequence YYAVAVVKKD description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YlSVAVVKKS source prosite : PS00205 14) chain C residue 188-204 type prosite sequence YSGAFKCLKDGAGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YtGAFRCLvek.GDVAF source prosite : PS00206 15) chain C residue 222-252 type prosite sequence QYELLCLDNTRKPVDEYKDCHLAQVPSHTVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. DFeLLClDgtrkp...VseahnChlAkapnHaVV source prosite : PS00207 16) chain C residue 63 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 17) chain C residue 95 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 188 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 249 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 120 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 21) chain C residue 124 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 22) chain C residue 126 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 23) chain C residue 127 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 24) chain C residue 23 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:P12346 source Swiss-Prot : SWS_FT_FI3 25) chain C residue 32 type CARBOHYD sequence S description O-linked (GalNAc...) serine source Swiss-Prot : SWS_FT_FI4

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