Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005623 | cellular_component | obsolete cell |
A | 0005769 | cellular_component | early endosome |
A | 0005886 | cellular_component | plasma membrane |
A | 0006826 | biological_process | iron ion transport |
A | 0006880 | biological_process | intracellular sequestering of iron ion |
A | 0006881 | biological_process | extracellular sequestering of iron ion |
A | 0006953 | biological_process | acute-phase response |
A | 0008199 | molecular_function | ferric iron binding |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0019730 | biological_process | antimicrobial humoral response |
A | 0019731 | biological_process | antibacterial humoral response |
A | 0032496 | biological_process | response to lipopolysaccharide |
A | 0046872 | molecular_function | metal ion binding |
A | 0055037 | cellular_component | recycling endosome |
A | 1990377 | cellular_component | organomineral extracellular matrix |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE AL A 687 |
Chain | Residue |
A | ASP60 |
A | TYR92 |
A | TYR191 |
A | HIS250 |
A | BCT688 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BCT A 688 |
Chain | Residue |
A | SER122 |
A | ALA123 |
A | GLY124 |
A | TYR191 |
A | HIS250 |
A | AL687 |
A | ASP60 |
A | TYR92 |
A | THR117 |
A | ARG121 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE AL A 689 |
Chain | Residue |
A | ASP395 |
A | TYR431 |
A | TYR524 |
A | HIS592 |
A | BCT690 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BCT A 690 |
Chain | Residue |
A | ASP395 |
A | TYR431 |
A | THR456 |
A | ARG460 |
A | THR461 |
A | ALA462 |
A | GLY463 |
A | TYR524 |
A | HIS592 |
A | AL689 |
Functional Information from PROSITE/UniProt
site_id | PS00205 |
Number of Residues | 10 |
Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG |
Chain | Residue | Details |
A | TYR92-GLY101 | |
A | TYR431-ASP440 | |
site_id | PS00206 |
Number of Residues | 17 |
Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFHCLkdgkGDVAF |
Chain | Residue | Details |
A | TYR191-PHE207 | |
A | TYR524-PHE539 | |
site_id | PS00207 |
Number of Residues | 31 |
Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLClDgsrqp...VdnyktCnwArvaaHaVV |
Chain | Residue | Details |
A | GLU223-VAL253 | |
A | ASP565-VAL595 | |
site_id | PS00962 |
Number of Residues | 12 |
Details | RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. VpSLMDSQLYLG |
Chain | Residue | Details |
A | VAL310-GLY321 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP60 | |
A | TYR431 | |
A | THR456 | |
A | ARG460 | |
A | ALA462 | |
A | GLY463 | |
A | TYR524 | |
A | HIS592 | |
A | TYR92 | |
A | THR117 | |
A | ARG121 | |
A | ALA123 | |
A | GLY124 | |
A | TYR191 | |
A | HIS250 | |
A | ASP395 | |
Chain | Residue | Details |
A | ASN473 | |