Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005769 | cellular_component | early endosome |
A | 0005886 | cellular_component | plasma membrane |
A | 0006826 | biological_process | iron ion transport |
A | 0019731 | biological_process | antibacterial humoral response |
A | 0046872 | molecular_function | metal ion binding |
A | 0055037 | cellular_component | recycling endosome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CO3 A 700 |
Chain | Residue |
A | ASP63 |
A | TYR95 |
A | THR120 |
A | ARG124 |
A | ALA126 |
A | GLY127 |
A | TYR188 |
A | HIS249 |
A | FE702 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CO3 A 701 |
Chain | Residue |
A | ASP392 |
A | TYR425 |
A | THR451 |
A | ARG455 |
A | THR456 |
A | ALA457 |
A | GLY458 |
A | TYR514 |
A | HIS582 |
A | FE703 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 702 |
Chain | Residue |
A | ASP63 |
A | TYR95 |
A | TYR188 |
A | HIS249 |
A | CO3700 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 703 |
Chain | Residue |
A | ASP392 |
A | TYR425 |
A | TYR514 |
A | HIS582 |
A | CO3701 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 800 |
Chain | Residue |
A | ARG124 |
A | GLY187 |
A | TYR188 |
A | HOH803 |
Functional Information from PROSITE/UniProt
site_id | PS00205 |
Number of Residues | 10 |
Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YlSVAVVKKS |
Chain | Residue | Details |
A | TYR425-SER434 | |
site_id | PS00206 |
Number of Residues | 17 |
Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdglGDVAF |
Chain | Residue | Details |
A | TYR188-PHE204 | |
A | TYR514-PHE529 | |
site_id | PS00207 |
Number of Residues | 31 |
Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeyeqChlArvpsHaVV |
Chain | Residue | Details |
A | GLN222-VAL252 | |
A | ASP555-VAL585 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP63 | |
A | TYR425 | |
A | THR451 | |
A | ARG455 | |
A | ALA457 | |
A | GLY458 | |
A | TYR514 | |
A | HIS582 | |
A | TYR95 | |
A | THR120 | |
A | ARG124 | |
A | ALA126 | |
A | GLY127 | |
A | TYR188 | |
A | HIS249 | |
A | ASP392 | |
Chain | Residue | Details |
A | ARG23 | |
Chain | Residue | Details |
A | SER370 | |
A | SER663 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN490 | |