1VFD
HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY GLU (R121E)
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 A 400 |
| Chain | Residue |
| A | ASP60 |
| A | TYR92 |
| A | TYR192 |
| A | HIS253 |
| A | CO3401 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 A 401 |
| Chain | Residue |
| A | ASP60 |
| A | TYR92 |
| A | THR117 |
| A | GLU121 |
| A | ALA123 |
| A | TYR192 |
| A | HIS253 |
| A | FE400 |
| A | HOH519 |
| site_id | BST |
| Number of Residues | 10 |
| Details | METAL AND ANION BINDING SITE. |
| Chain | Residue |
| A | ASP60 |
| A | CO3401 |
| A | TYR92 |
| A | THR117 |
| A | GLU121 |
| A | ALA123 |
| A | GLY124 |
| A | TYR192 |
| A | HIS253 |
| A | FE400 |
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 | TYR72 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:12535064 |
| Chain | Residue | Details |
| A | ARG258 |
| 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 | LEU59 | |
| A | HIS91 | |
| A | SER191 | |
| A | SER252 |
| 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 | HIS116 | |
| A | ARG120 | |
| A | THR122 | |
| A | ALA123 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Interaction with PspA |
| Chain | Residue | Details |
| A | ARG3 | |
| A | SER12 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Important for iron binding |
| Chain | Residue | Details |
| A | ILE209 |
| 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 | LEU136 |
