eF-site ID 6d04-D PDB Code 6d04 Chain D click to enlarge Title Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; two molecules of parasite ligand, subclass 1. Classification CELL INVASION Compound Transferrin receptor protein 1 Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence D:  VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACV KKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPV VAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHT GLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAP CADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAG DVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKD CHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSK EFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYV TAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSV NSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAG KCGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLT WDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFF SEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGA FRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYE LLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKI LRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAK LHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP Description (1)  Transferrin receptor protein 1, Serotransferrin, Reticulocyte binding protein 2, putative Functional site 1) chain D residue 63 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 2) chain D residue 95 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 3) chain D residue 188 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 249 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 120 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 6) chain D residue 124 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 7) chain D residue 126 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 8) chain D residue 127 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 9) chain D 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 10) chain D 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 11) chain D 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 12) chain D 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 13) chain D 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 14) chain D 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 15) chain D residue 452 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 16) chain D residue 456 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 17) chain D residue 458 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 18) chain D residue 459 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 19) chain D residue 23 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:P12346 source Swiss-Prot : SWS_FT_FI5 20) chain D residue 370 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI6 21) chain D residue 666 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI6 22) chain D residue 32 type CARBOHYD sequence S description O-linked (GalNAc...) serine source Swiss-Prot : SWS_FT_FI7 23) chain D 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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