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 | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02770 |
Chain | Residue | Details |
A | HIS3 | |
B | HIS3 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V03 |
Chain | Residue | Details |
A | GLU6 | |
B | GLU6 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:23769932, ECO:0007744|PDB:3V03, ECO:0007744|PDB:4JK4 |
Chain | Residue | Details |
A | ASP13 | |
B | ASP258 | |
A | GLU243 | |
A | GLU251 | |
A | ASP254 | |
A | ASP258 | |
B | ASP13 | |
B | GLU243 | |
B | GLU251 | |
B | ASP254 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02768 |
Chain | Residue | Details |
A | HIS67 | |
A | HIS246 | |
A | ASP248 | |
B | HIS67 | |
B | HIS246 | |
B | ASP248 |
site_id | SWS_FT_FI5 |
Number of Residues | 10 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02768 |
Chain | Residue | Details |
A | SER5 | |
B | SER488 | |
A | SER58 | |
A | SER65 | |
A | SER418 | |
A | SER488 | |
B | SER5 | |
B | SER58 | |
B | SER65 | |
B | SER418 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02768 |
Chain | Residue | Details |
A | THR83 | |
A | THR419 | |
A | THR421 | |
B | THR83 | |
B | THR419 | |
B | THR421 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724 |
Chain | Residue | Details |
A | LYS204 | |
A | LYS563 | |
B | LYS204 | |
B | LYS563 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724 |
Chain | Residue | Details |
A | SER272 | |
B | SER272 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P02768 |
Chain | Residue | Details |
A | LYS533 | |
B | LYS533 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02770 |
Chain | Residue | Details |
A | THR545 | |
B | THR545 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:21565706 |
Chain | Residue | Details |
A | LYS127 | |
B | LYS127 |