1H44
R210L N-TERMINAL LOBE HUMAN LACTOFERRIN
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A1326 |
Chain | Residue |
A | ASP60 |
A | TYR92 |
A | TYR192 |
A | HIS253 |
A | CO31327 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CO3 A1327 |
Chain | Residue |
A | THR122 |
A | ALA123 |
A | GLY124 |
A | TYR192 |
A | FE1326 |
A | ASP60 |
A | TYR92 |
A | THR117 |
A | ARG121 |
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 |
site_id | PS00206 |
Number of Residues | 17 |
Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLrdgaGDVAF |
Chain | Residue | Details |
A | TYR192-PHE208 |
site_id | PS00207 |
Number of Residues | 31 |
Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV |
Chain | Residue | Details |
A | GLU226-VAL256 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:12535064 |
Chain | Residue | Details |
A | LYS73 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:12535064 |
Chain | Residue | Details |
A | SER259 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72 |
Chain | Residue | Details |
A | ASP60 | |
A | TYR92 | |
A | TYR192 | |
A | HIS253 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72 |
Chain | Residue | Details |
A | THR117 | |
A | ARG121 | |
A | ALA123 | |
A | GLY124 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Interaction with PspA |
Chain | Residue | Details |
A | ARG4 | |
A | GLN13 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Important for iron binding |
Chain | Residue | Details |
A | LEU210 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15299444, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:8069634, ECO:0000269|Ref.72 |
Chain | Residue | Details |
A | ASN137 |