eF-site ID 6d05-ABCDEF
PDB Code 6d05
Chain A, B, C, D, E, F
Title Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; two molecules of parasite ligand, subclass 2.
Classification CELL INVASION
Compound Transferrin receptor protein 1
Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  FRLYWDDLKRKLSEKLDSTDFTSTIKLLNENSYVPREAGS
QKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNS
VIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGT
KKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGV
LIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHT
QFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKT
DSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEP
DHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLK
DGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAF
TYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTG
QFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCE
DTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVI
KLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSL
QWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVM
RVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLR
KQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNE
F
B:  FRLYWDDLKRKLSEKLDSTDFTSTIKLLNENSYVPREAGS
QKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNS
VIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGT
KKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGV
LIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHT
QFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKT
DSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEP
DHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLK
DGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAF
TYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTG
QFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCE
DTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVI
KLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSL
QWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVM
RVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLR
KQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNE
F
C:  VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACV
KKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPV
VAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHT
GLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAP
CADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAG
DVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKD
CHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSK
EFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYV
TAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSV
NSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAG
KCGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLT
WDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFF
SEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGA
FRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYE
LLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKI
LRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAK
LHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
D:  VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACV
KKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPV
VAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHT
GLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAP
CADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAG
DVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKD
CHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSK
EFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYV
TAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSV
NSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAG
KCGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLT
WDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFF
SEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGA
FRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYE
LLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKI
LRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAK
LHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
E:  STNTTDNIDYFDISDESNYYLISQLRPHFSNIYFFDEFKR
YASYHTEIKRYEDIHKTKVNSLLNEASRAIGICNRAKNTV
KGLINILENPQKFKTQRESYDVKLRQYEEKKEAFRGCLLN
KNRKNLDQIKKINNEIRDLLEKLKCSQDCQTNVYFDMIKI
YLVDFKKMPYENYDTFIKQYKNSYLSGVDMIRKIEKQIDN
PVTINAIKFTQKEMGYIIDRFEYHLQKVKHSIDQVTALSD
GVKPKQVTKNRLKEYYFNIGNYYSIFKFGKDSLNMLNKAL
IHKEKIVHNLLGELFGHLEERISKLIDSEYFITESNNIIS
QSEETLKLAEDVYDKNTKLIEDLTLYPHLEINEFKKDYDN
NVEDLRESIIYIQSYVSSIKSAYRYNVLEKDSVESKQKNI
PANSNAQKKVDELLSIIDSISYSNFSVAENFQKMKDYYKE
IEKLKIKILQLIEAIKKYQQHVEELI
F:  STNTTDNIDYFDISDESNYYLISQLRPHFSNIYFFDEFKR
YASYHTEIKRYEDIHKTKVNSLLNEASRAIGICNRAKNTV
KGLINILENPQKFKTQRESYDVKLRQYEEKKEAFRGCLLN
KNRKNLDQIKKINNEIRDLLEKLKCSQDCQTNVYFDMIKI
YLVDFKKMPYENYDTFIKQYKNSYLSGVDMIRKIEKQIDN
PVTINAIKFTQKEMGYIIDRFEYHLQKVKHSIDQVTALSD
GVKPKQVTKNRLKEYYFNIGNYYSIFKFGKDSLNMLNKAL
IHKEKIVHNLLGELFGHLEERISKLIDSEYFITESNNIIS
QSEETLKLAEDVYDKNTKLIEDLTLYPHLEINEFKKDYDN
NVEDLRESIIYIQSYVSSIKSAYRYNVLEKDSVESKQKNI
PANSNAQKKVDELLSIIDSISYSNFSVAENFQKMKDYYKE
IEKLKIKILQLIEAIKKYQQHVEELI
Description (1)  Transferrin receptor protein 1, Serotransferrin, Reticulocyte binding protein 2, putative


Functional site
1) chain C
residue 63
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
2) chain C
residue 95
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
3) chain C
residue 188
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
4) chain C
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 63
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
6) chain D
residue 95
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
7) chain D
residue 188
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
8) chain D
residue 249
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
9) chain C
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
10) 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
11) chain C
residue 120
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2
12) chain C
residue 124
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2
13) chain C
residue 126
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2
14) chain C
residue 127
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2
15) chain D
residue 120
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2
16) chain D
residue 124
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2
17) chain D
residue 126
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2
18) chain D
residue 127
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2
19) chain C
residue 452
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
20) chain C
residue 456
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
21) chain C
residue 458
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
22) chain C
residue 459
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
23) chain D
residue 452
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
24) chain D
residue 456
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
25) chain D
residue 458
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
26) chain D
residue 459
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
27) chain C
residue 23
type MOD_RES
sequence R
description Dimethylated arginine => ECO:0000250|UniProtKB:P12346
source Swiss-Prot : SWS_FT_FI5
28) chain D
residue 23
type MOD_RES
sequence R
description Dimethylated arginine => ECO:0000250|UniProtKB:P12346
source Swiss-Prot : SWS_FT_FI5
29) chain C
residue 370
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI6
30) chain C
residue 666
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI6
31) chain D
residue 370
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI6
32) chain D
residue 666
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI6
33) chain C
residue 32
type CARBOHYD
sequence S
description O-linked (GalNAc...) serine
source Swiss-Prot : SWS_FT_FI7
34) chain D
residue 32
type CARBOHYD
sequence S
description O-linked (GalNAc...) serine
source Swiss-Prot : SWS_FT_FI7
35) chain C
residue 472
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627
source Swiss-Prot : SWS_FT_FI9
36) 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
37) chain C
residue 95-104
type prosite
sequence YYAVAVVKKD
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
source prosite : PS00205
38) chain C
residue 426-435
type prosite
sequence YFAVAVVKKS
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
source prosite : PS00205
39) chain C
residue 188-204
type prosite
sequence YSGAFKCLKDGAGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
source prosite : PS00206
40) chain C
residue 517-532
type prosite
sequence YTGAFRCLVEKGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
source prosite : PS00206
41) chain C
residue 222-252
type prosite
sequence QYELLCLDNTRKPVDEYKDCHLAQVPSHTVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
source prosite : PS00207
42) chain C
residue 558-588
type prosite
sequence DYELLCLDGTRKPVEEYANCHLARAPNHAVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
source prosite : PS00207
43) chain C
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
44) chain C
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
45) chain C
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
46) chain C
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
47) 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
48) 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
49) 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
50) 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
51) chain C
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
52) 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

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