eF-site ID 4x1d-B PDB Code 4x1d Chain B click to enlarge Title Ytterbium-bound human serum transferrin Classification METAL TRANSPORT Compound Serotransferrin Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence B:  DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKK ASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVA EFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGL GRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCA DGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDV AFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCH LAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEF QLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTA IRNLREGTCPECKPVKWCALSHHERLKCDEWSVNSVGKIE CVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPV LAENYNKPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAV GRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSL CKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVK HQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEY ANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNFCL FRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGN LRKCSTSSLLEACTFRRP Description Functional site 1) chain B residue 392 type sequence D description binding site for residue YB B 701 source : AC4 2) chain B residue 426 type sequence Y description binding site for residue YB B 701 source : AC4 3) chain B residue 517 type sequence Y description binding site for residue YB B 701 source : AC4 4) chain B residue 585 type sequence H description binding site for residue YB B 701 source : AC4 5) chain B residue 392 type sequence D description binding site for residue MLI B 702 source : AC5 6) chain B residue 426 type sequence Y description binding site for residue MLI B 702 source : AC5 7) chain B residue 452 type sequence T description binding site for residue MLI B 702 source : AC5 8) chain B residue 456 type sequence R description binding site for residue MLI B 702 source : AC5 9) chain B residue 457 type sequence T description binding site for residue MLI B 702 source : AC5 10) chain B residue 458 type sequence A description binding site for residue MLI B 702 source : AC5 11) chain B residue 459 type sequence G description binding site for residue MLI B 702 source : AC5 12) chain B residue 517 type sequence Y description binding site for residue MLI B 702 source : AC5 13) chain B residue 585 type sequence H description binding site for residue MLI B 702 source : AC5 14) chain B residue 228 type sequence L description binding site for residue GOL B 703 source : AC6 15) chain B residue 229 type sequence D description binding site for residue GOL B 703 source : AC6 16) chain B residue 240 type sequence D description binding site for residue GOL B 703 source : AC6 17) chain B residue 242 type sequence H description binding site for residue GOL B 703 source : AC6 18) chain B 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 19) chain B residue 452 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 20) chain B residue 456 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 458 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 459 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 370 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI6 24) chain B residue 666 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI6 25) chain B residue 472 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627 source Swiss-Prot : SWS_FT_FI9 26) chain B residue 63 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 95 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 188 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 249 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 120 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 31) chain B residue 124 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 32) chain B residue 126 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 33) chain B residue 127 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 34) chain B residue 23 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:P12346 source Swiss-Prot : SWS_FT_FI5 35) chain B residue 32 type CARBOHYD sequence S description O-linked (GalNAc...) serine source Swiss-Prot : SWS_FT_FI7 36) chain B 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 37) chain B 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 38) chain B 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 39) chain B 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 40) chain B 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

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