5X5P
Human serum transferrin bound to ruthenium NTA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005768 | cellular_component | endosome |
| A | 0005769 | cellular_component | early endosome |
| A | 0005770 | cellular_component | late endosome |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005905 | cellular_component | clathrin-coated pit |
| A | 0006826 | biological_process | iron ion transport |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0007015 | biological_process | actin filament organization |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0009617 | biological_process | response to bacterium |
| A | 0009925 | cellular_component | basal plasma membrane |
| A | 0009986 | cellular_component | cell surface |
| A | 0010008 | cellular_component | endosome membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0019731 | biological_process | antibacterial humoral response |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0030139 | cellular_component | endocytic vesicle |
| A | 0030316 | biological_process | osteoclast differentiation |
| A | 0030669 | cellular_component | clathrin-coated endocytic vesicle membrane |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0031647 | biological_process | regulation of protein stability |
| A | 0031982 | cellular_component | vesicle |
| A | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
| A | 0034756 | biological_process | regulation of iron ion transport |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0034986 | molecular_function | iron chaperone activity |
| A | 0042327 | biological_process | positive regulation of phosphorylation |
| A | 0044325 | molecular_function | transmembrane transporter binding |
| A | 0045178 | cellular_component | basal part of cell |
| A | 0045780 | biological_process | positive regulation of bone resorption |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048260 | biological_process | positive regulation of receptor-mediated endocytosis |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0055037 | cellular_component | recycling endosome |
| A | 0060586 | biological_process | multicellular organismal-level iron ion homeostasis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070371 | biological_process | ERK1 and ERK2 cascade |
| A | 0071281 | biological_process | cellular response to iron ion |
| A | 0072562 | cellular_component | blood microparticle |
| A | 1990459 | molecular_function | transferrin receptor binding |
| A | 1990712 | cellular_component | HFE-transferrin receptor complex |
| A | 2000147 | biological_process | positive regulation of cell motility |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue MLI A 701 |
| Chain | Residue |
| A | ASP392 |
| A | FE702 |
| A | TYR426 |
| A | THR452 |
| A | ARG456 |
| A | THR457 |
| A | ALA458 |
| A | GLY459 |
| A | TYR517 |
| A | HIS585 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue FE A 702 |
| Chain | Residue |
| A | ASP392 |
| A | TYR426 |
| A | TYR517 |
| A | HIS585 |
| A | MLI701 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue RU A 703 |
| Chain | Residue |
| A | HIS14 |
| A | NTA707 |
| A | HOH803 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue RU A 704 |
| Chain | Residue |
| A | HIS578 |
| A | NTA708 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue RU A 705 |
| Chain | Residue |
| A | HIS273 |
| A | HOH804 |
| A | HOH808 |
| A | HOH809 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue RU A 706 |
| Chain | Residue |
| A | HIS289 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue NTA A 707 |
| Chain | Residue |
| A | HIS14 |
| A | HIS289 |
| A | RU703 |
| A | HOH803 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue NTA A 708 |
| Chain | Residue |
| A | HIS578 |
| A | ARG581 |
| A | RU704 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 709 |
| Chain | Residue |
| A | SER125 |
| A | ASN129 |
| A | TYR319 |
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 |
| A | TYR95-ASP104 |
| site_id | PS00206 |
| Number of Residues | 17 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF |
| Chain | Residue | Details |
| A | TYR188-PHE204 | |
| A | TYR517-PHE532 |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV |
| Chain | Residue | Details |
| A | GLN222-VAL252 | |
| A | ASP558-VAL588 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 |
| Chain | Residue | Details |
| A | ASP63 | |
| A | TYR95 | |
| A | TYR188 | |
| A | HIS249 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR120 | |
| A | ARG124 | |
| A | ALA126 | |
| A | GLY127 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 |
| A | ASP392 | |
| A | TYR426 | |
| A | TYR517 | |
| A | HIS585 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 |
| Chain | Residue | Details |
| A | THR452 | |
| A | ARG456 | |
| A | ALA458 | |
| A | GLY459 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:P12346 |
| Chain | Residue | Details |
| A | ARG23 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 |
| Chain | Residue | Details |
| A | SER370 | |
| A | SER666 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GalNAc...) serine |
| Chain | Residue | Details |
| A | SER32 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| 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 |
| A | ASN413 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627 |
| Chain | Residue | Details |
| A | ASN472 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| 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 |
| A | ASN611 |
