8WDD
Crystal structure of BSA in complex with B1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009267 | biological_process | cellular response to starvation |
| A | 0015643 | molecular_function | toxic substance binding |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031667 | biological_process | response to nutrient levels |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051902 | biological_process | negative regulation of mitochondrial depolarization |
| A | 0072732 | biological_process | cellular response to calcium ion starvation |
| A | 1903981 | molecular_function | enterobactin binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0005504 | molecular_function | fatty acid binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0008289 | molecular_function | lipid binding |
| B | 0009267 | biological_process | cellular response to starvation |
| B | 0015643 | molecular_function | toxic substance binding |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0031667 | biological_process | response to nutrient levels |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051902 | biological_process | negative regulation of mitochondrial depolarization |
| B | 0072732 | biological_process | cellular response to calcium ion starvation |
| B | 1903981 | molecular_function | enterobactin binding |
Functional Information from PROSITE/UniProt
| site_id | PS00212 |
| Number of Residues | 25 |
| Details | ALBUMIN_1 Albumin domain signature. YngvfqeCCqaEdkgaCLlpkietM |
| Chain | Residue | Details |
| A | TYR160-MET184 | |
| A | TYR352-LEU376 | |
| A | PHE550-LEU574 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 384 |
| Details | Domain: {"description":"Albumin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 394 |
| Details | Domain: {"description":"Albumin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P02770","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22677715","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V03","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22677715","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23769932","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JK4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P02768","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P02768","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P02768","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P02768","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P02770","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"21565706","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
