eF-site ID 4x1d-A PDB Code 4x1d Chain A click to enlarge Title Ytterbium-bound human serum transferrin Classification METAL TRANSPORT Compound Serotransferrin Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKK ASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVA EFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGL GRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCA DGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDV AFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCH LAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEF QLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTA IRNLREGTCPECKPVKWCALSHHERLKCDEWSVNSVGKIE CVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPV LAENYNKPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAV GRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSL CKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVK HQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEY ANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNFCL FRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGN LRKCSTSSLLEACTFRRP Description Functional site 1) chain A residue 392 type sequence D description binding site for residue YB A 701 source : AC1 2) chain A residue 426 type sequence Y description binding site for residue YB A 701 source : AC1 3) chain A residue 517 type sequence Y description binding site for residue YB A 701 source : AC1 4) chain A residue 585 type sequence H description binding site for residue YB A 701 source : AC1 5) chain A residue 392 type sequence D description binding site for residue MLI A 702 source : AC2 6) chain A residue 426 type sequence Y description binding site for residue MLI A 702 source : AC2 7) chain A residue 452 type sequence T description binding site for residue MLI A 702 source : AC2 8) chain A residue 456 type sequence R description binding site for residue MLI A 702 source : AC2 9) chain A residue 457 type sequence T description binding site for residue MLI A 702 source : AC2 10) chain A residue 458 type sequence A description binding site for residue MLI A 702 source : AC2 11) chain A residue 459 type sequence G description binding site for residue MLI A 702 source : AC2 12) chain A residue 517 type sequence Y description binding site for residue MLI A 702 source : AC2 13) chain A residue 585 type sequence H description binding site for residue MLI A 702 source : AC2 14) chain A residue 227 type sequence C description binding site for residue GOL A 703 source : AC3 15) chain A residue 228 type sequence L description binding site for residue GOL A 703 source : AC3 16) chain A residue 229 type sequence D description binding site for residue GOL A 703 source : AC3 17) chain A residue 240 type sequence D description binding site for residue GOL A 703 source : AC3 18) chain A residue 242 type sequence H description binding site for residue GOL A 703 source : AC3 19) chain A residue 95-104 type prosite sequence YYAVAVVKKD description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD source prosite : PS00205 20) chain A residue 426-435 type prosite sequence YFAVAVVKKS description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD source prosite : PS00205 21) chain A residue 188-204 type prosite sequence YSGAFKCLKDGAGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF source prosite : PS00206 22) chain A residue 517-532 type prosite sequence YTGAFRCLVEKGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF source prosite : PS00206 23) chain A residue 222-252 type prosite sequence QYELLCLDNTRKPVDEYKDCHLAQVPSHTVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV source prosite : PS00207 24) chain A residue 558-588 type prosite sequence DYELLCLDGTRKPVEEYANCHLARAPNHAVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV source prosite : PS00207 25) chain A residue 413 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ source Swiss-Prot : SWS_FT_FI8 26) chain A residue 63 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 95 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 188 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 249 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 120 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 31) chain A residue 124 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 32) chain A residue 126 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 33) chain A residue 127 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 23 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:P12346 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 370 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI6 36) chain A residue 666 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI6 37) chain A residue 32 type CARBOHYD sequence S description O-linked (GalNAc...) serine source Swiss-Prot : SWS_FT_FI7 38) chain A residue 611 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295 source Swiss-Prot : SWS_FT_FI10 39) chain A residue 517 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ source Swiss-Prot : SWS_FT_FI3 40) chain A residue 585 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ source Swiss-Prot : SWS_FT_FI3 41) chain A residue 392 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ source Swiss-Prot : SWS_FT_FI3 42) chain A residue 426 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ source Swiss-Prot : SWS_FT_FI3 43) chain A residue 458 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 459 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 452 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 456 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 47) chain A residue 472 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627 source Swiss-Prot : SWS_FT_FI9

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