4X1B
Human serum transferrin with ferric ion bound at the C-lobe only
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 | 5 |
Details | binding site for residue FE A 701 |
Chain | Residue |
A | ASP392 |
A | TYR426 |
A | TYR517 |
A | HIS585 |
A | MLI702 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue MLI A 702 |
Chain | Residue |
A | ALA458 |
A | GLY459 |
A | TYR517 |
A | HIS585 |
A | FE701 |
A | HOH893 |
A | ASP392 |
A | TYR426 |
A | THR452 |
A | ARG456 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL A 703 |
Chain | Residue |
A | CYS227 |
A | LEU228 |
A | ASP229 |
A | HIS242 |
A | LYS591 |
A | HOH937 |
A | HOH970 |
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 | |
A | TYR426-SER435 |
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 |