6D05
Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; two molecules of parasite ligand, subclass 2.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004998 | molecular_function | transferrin receptor activity |
| A | 0033572 | biological_process | transferrin transport |
| B | 0004998 | molecular_function | transferrin receptor activity |
| B | 0033572 | biological_process | transferrin transport |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0006826 | biological_process | iron ion transport |
| C | 0006879 | biological_process | intracellular iron ion homeostasis |
| C | 0008199 | molecular_function | ferric iron binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0006826 | biological_process | iron ion transport |
| D | 0006879 | biological_process | intracellular iron ion homeostasis |
| D | 0008199 | molecular_function | ferric iron binding |
Functional Information from PROSITE/UniProt
| site_id | PS00205 |
| Number of Residues | 10 |
| Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD |
| Chain | Residue | Details |
| C | TYR95-ASP104 | |
| C | TYR426-SER435 |
| site_id | PS00206 |
| Number of Residues | 17 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF |
| Chain | Residue | Details |
| C | TYR188-PHE204 | |
| C | TYR517-PHE532 |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV |
| Chain | Residue | Details |
| C | GLN222-VAL252 | |
| C | ASP558-VAL588 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 |
| Chain | Residue | Details |
| C | ASP63 | |
| C | TYR95 | |
| C | TYR188 | |
| C | HIS249 | |
| D | ASP63 | |
| D | TYR95 | |
| D | TYR188 | |
| D | HIS249 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | THR120 | |
| C | ARG124 | |
| C | ALA126 | |
| C | GLY127 | |
| D | THR120 | |
| D | ARG124 | |
| D | ALA126 | |
| D | GLY127 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: 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 |
| Chain | Residue | Details |
| C | ASP392 | |
| C | TYR426 | |
| C | TYR517 | |
| C | HIS585 | |
| D | ASP392 | |
| D | TYR426 | |
| D | TYR517 | |
| D | HIS585 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 |
| Chain | Residue | Details |
| C | THR452 | |
| C | ARG456 | |
| C | ALA458 | |
| C | GLY459 | |
| D | THR452 | |
| D | ARG456 | |
| D | ALA458 | |
| D | GLY459 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:P12346 |
| Chain | Residue | Details |
| C | ARG23 | |
| D | ARG23 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 |
| Chain | Residue | Details |
| C | SER370 | |
| C | SER666 | |
| D | SER370 | |
| D | SER666 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GalNAc...) serine |
| Chain | Residue | Details |
| C | SER32 | |
| D | SER32 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: 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 |
| Chain | Residue | Details |
| C | ASN413 | |
| D | ASN413 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627 |
| Chain | Residue | Details |
| C | ASN472 | |
| D | ASN472 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: 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 |
| Chain | Residue | Details |
| C | ASN611 | |
| D | ASN611 |
