3V03
Crystal structure of Bovine Serum Albumin
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 | 0005737 | cellular_component | cytoplasm |
| 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 | 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 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 PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 584 |
| Chain | Residue |
| A | GLU6 |
| A | ASP248 |
| A | GLU251 |
| A | HOH589 |
| A | HOH591 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 585 |
| Chain | Residue |
| A | HOH604 |
| A | SER109 |
| A | ASP111 |
| A | HOH592 |
| A | HOH593 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 586 |
| Chain | Residue |
| A | ASP13 |
| A | ASP254 |
| A | ASP258 |
| A | HOH605 |
| A | HOH607 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 584 |
| Chain | Residue |
| B | SER109 |
| B | ASP111 |
| B | HOH589 |
| B | HOH590 |
| B | HOH591 |
| B | HOH592 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 585 |
| Chain | Residue |
| B | GLU243 |
| B | ASP248 |
| B | GLU251 |
| B | HOH606 |
| B | HOH607 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 586 |
| Chain | Residue |
| B | ASP13 |
| B | ASP254 |
| B | ASP258 |
| B | HOH593 |
| B | HOH594 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT B 587 |
| Chain | Residue |
| B | GLU48 |
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 |
| B | GLU243 | |
| B | GLU251 | |
| B | ASP254 | |
| B | ASP258 | |
| A | ASP13 | |
| A | GLU243 | |
| A | GLU251 | |
| A | ASP254 | |
| A | ASP258 | |
| B | ASP13 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02768 |
| Chain | Residue | Details |
| A | ASP248 | |
| B | HIS67 | |
| B | HIS246 | |
| B | ASP248 | |
| A | HIS67 | |
| A | HIS246 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02768 |
| Chain | Residue | Details |
| A | SER488 | |
| B | SER5 | |
| B | SER58 | |
| B | SER65 | |
| B | SER418 | |
| B | SER488 | |
| A | SER65 | |
| A | SER418 | |
| A | SER5 | |
| A | SER58 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02768 |
| Chain | Residue | Details |
| A | THR421 | |
| B | THR83 | |
| B | THR419 | |
| B | THR421 | |
| A | THR83 | |
| A | THR419 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724 |
| Chain | Residue | Details |
| B | LYS204 | |
| B | LYS563 | |
| A | LYS204 | |
| A | 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 |
| B | LYS127 | |
| A | LYS127 |
