1L5T
Crystal Structure of a Domain-Opened Mutant (R121D) of the Human Lactoferrin N-lobe Refined From a Merohedrally-Twinned Crystal Form.
Functional Information from GO Data
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 | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:12535064 |
| Chain | Residue | Details |
| A | LYS73 | |
| B | LYS73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:12535064 |
| Chain | Residue | Details |
| A | SER259 | |
| B | SER259 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| 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 | |
| B | ASP60 | |
| B | TYR92 | |
| B | TYR192 | |
| B | HIS253 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| 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 | ASP121 | |
| A | ALA123 | |
| A | GLY124 | |
| B | THR117 | |
| B | ASP121 | |
| B | ALA123 | |
| B | GLY124 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Interaction with PspA |
| Chain | Residue | Details |
| A | ARG4 | |
| A | GLN13 | |
| B | ARG4 | |
| B | GLN13 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Important for iron binding |
| Chain | Residue | Details |
| A | ARG210 | |
| B | ARG210 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| 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 | |
| B | ASN137 |
