eF-site ID 6d05-C
PDB Code 6d05
Chain C

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 2.
Classification CELL INVASION
Compound Transferrin receptor protein 1
Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence C:  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 C
residue 95-104
type prosite
sequence YYAVAVVKKD
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
source prosite : PS00205
2) chain C
residue 426-435
type prosite
sequence YFAVAVVKKS
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
source prosite : PS00205
3) chain C
residue 188-204
type prosite
sequence YSGAFKCLKDGAGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
source prosite : PS00206
4) chain C
residue 517-532
type prosite
sequence YTGAFRCLVEKGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
source prosite : PS00206
5) chain C
residue 222-252
type prosite
sequence QYELLCLDNTRKPVDEYKDCHLAQVPSHTVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
source prosite : PS00207
6) chain C
residue 558-588
type prosite
sequence DYELLCLDGTRKPVEEYANCHLARAPNHAVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
source prosite : PS00207
7) chain C
residue 370
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI6
8) chain C
residue 666
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI6
9) chain C
residue 32
type CARBOHYD
sequence S
description O-linked (GalNAc...) serine
source Swiss-Prot : SWS_FT_FI7
10) 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
11) 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
12) 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
13) 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
14) 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
15) chain C
residue 458
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
16) chain C
residue 459
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
17) chain C
residue 452
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
18) chain C
residue 456
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI4
19) 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
20) chain C
residue 63
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
21) chain C
residue 95
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
22) chain C
residue 188
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
23) chain C
residue 249
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
source Swiss-Prot : SWS_FT_FI1
24) chain C
residue 126
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2
25) chain C
residue 127
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2
26) chain C
residue 120
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2
27) chain C
residue 124
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2
28) chain C
residue 23
type MOD_RES
sequence R
description Dimethylated arginine => ECO:0000250|UniProtKB:P12346
source Swiss-Prot : SWS_FT_FI5
29) 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

Display surface

Download
Links