2PMS
Crystal structure of the complex of human lactoferrin N-lobe and lactoferrin-binding domain of pneumococcal surface protein A
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 | TYR93-GLY102 |
| site_id | PS00206 |
| Number of Residues | 17 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLrdgaGDVAF |
| Chain | Residue | Details |
| A | TYR193-PHE209 |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV |
| Chain | Residue | Details |
| A | GLU227-VAL257 |
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 | LYS74 | |
| B | LYS74 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:12535064 |
| Chain | Residue | Details |
| A | SER260 | |
| B | SER260 |
| 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 | ASP61 | |
| A | TYR93 | |
| A | TYR193 | |
| A | HIS254 | |
| B | ASP61 | |
| B | TYR93 | |
| B | TYR193 | |
| B | HIS254 |
| 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 | THR118 | |
| A | ARG122 | |
| A | ALA124 | |
| A | GLY125 | |
| B | THR118 | |
| B | ARG122 | |
| B | ALA124 | |
| B | GLY125 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Interaction with PspA |
| Chain | Residue | Details |
| A | ARG5 | |
| A | GLN14 | |
| B | ARG5 | |
| B | GLN14 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Important for iron binding |
| Chain | Residue | Details |
| A | ARG211 | |
| B | ARG211 |
| 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 | ASN138 | |
| B | ASN138 |
