eF-site ID 3fgs-A PDB Code 3fgs Chain A click to enlarge Title Crystal structure of G65R/K206E double mutant of the N-lobe human transferrin Classification METAL TRANSPORT Compound Serotransferrin Source Homo sapiens (Human) (TRFE_HUMAN) Sequence A:  DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKK ASYLDCIRAIAANEADAVTLDARLVYDAYLAPNNLKPVVA EFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGL GRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCA DGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDV AFVEHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCH LAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEF QLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTA IRNLREGTC Description Functional site 1) chain A residue 63 type sequence D description BINDING SITE FOR RESIDUE CO3 A 401 source : AC1 2) chain A residue 95 type sequence Y description BINDING SITE FOR RESIDUE CO3 A 401 source : AC1 3) chain A residue 120 type sequence T description BINDING SITE FOR RESIDUE CO3 A 401 source : AC1 4) chain A residue 124 type sequence R description BINDING SITE FOR RESIDUE CO3 A 401 source : AC1 5) chain A residue 126 type sequence A description BINDING SITE FOR RESIDUE CO3 A 401 source : AC1 6) chain A residue 127 type sequence G description BINDING SITE FOR RESIDUE CO3 A 401 source : AC1 7) chain A residue 188 type sequence Y description BINDING SITE FOR RESIDUE CO3 A 401 source : AC1 8) chain A residue 249 type sequence H description BINDING SITE FOR RESIDUE CO3 A 401 source : AC1 9) chain A residue 63 type sequence D description BINDING SITE FOR RESIDUE FE A 402 source : AC2 10) chain A residue 95 type sequence Y description BINDING SITE FOR RESIDUE FE A 402 source : AC2 11) chain A residue 188 type sequence Y description BINDING SITE FOR RESIDUE FE A 402 source : AC2 12) chain A residue 249 type sequence H description BINDING SITE FOR RESIDUE FE A 402 source : AC2 13) chain A residue 63 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 95 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 188 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 249 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 120 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 18) chain A residue 124 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 19) chain A residue 126 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 20) chain A residue 127 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 21) chain A residue 23 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:P12346 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 32 type CARBOHYD sequence S description O-linked (GalNAc...) serine source Swiss-Prot : SWS_FT_FI4 23) chain A residue 95-104 type prosite sequence YYAVAVVKKD description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD source prosite : PS00205 24) chain A residue 188-204 type prosite sequence YSGAFKCLKDGAGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF source prosite : PS00206 25) chain A residue 222-252 type prosite sequence QYELLCLDNTRKPVDEYKDCHLAQVPSHTVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV source prosite : PS00207

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