4JK4
Crystal Structure of Bovine Serum Albumin in complex with 3,5-diiodosalicylic acid
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 PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DIU A 601 |
| Chain | Residue |
| A | TYR149 |
| A | ARG198 |
| A | ARG217 |
| A | LYS221 |
| A | HIS241 |
| A | ARG256 |
| A | ILE289 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DIU A 602 |
| Chain | Residue |
| A | ASN390 |
| A | ARG409 |
| A | GLU449 |
| A | LEU452 |
| A | ARG484 |
| A | SER488 |
| A | LEU386 |
| A | ILE387 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DIU A 603 |
| Chain | Residue |
| A | LEU115 |
| A | TYR137 |
| A | ILE141 |
| A | ARG185 |
| A | PEG605 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DIU A 604 |
| Chain | Residue |
| A | ARG194 |
| A | LEU197 |
| A | ARG198 |
| A | SER201 |
| A | TRP213 |
| A | ARG217 |
| A | ASP450 |
| A | HOH703 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 605 |
| Chain | Residue |
| A | LEU115 |
| A | PHE133 |
| A | TYR137 |
| A | TYR160 |
| A | DIU603 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 1PE A 606 |
| Chain | Residue |
| A | LYS573 |
| A | VAL576 |
| A | SER577 |
| A | THR580 |
| A | HOH742 |
| A | HOH742 |
| B | LYS573 |
| B | VAL576 |
| B | SER577 |
| B | THR580 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 607 |
| Chain | Residue |
| A | PHE205 |
| A | VAL215 |
| A | LYS350 |
| A | LEU480 |
| A | VAL481 |
| A | HOH754 |
| A | HOH779 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE A 608 |
| Chain | Residue |
| A | PHE506 |
| A | LYS524 |
| A | LEU531 |
| A | PHE550 |
| A | LEU574 |
| A | THR578 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 609 |
| Chain | Residue |
| A | GLU243 |
| A | ASP248 |
| A | GLU251 |
| A | CA610 |
| A | HOH763 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 610 |
| Chain | Residue |
| A | GLU251 |
| A | CA609 |
| A | HOH756 |
| A | HOH768 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 611 |
| Chain | Residue |
| A | ASP107 |
| A | SER109 |
| A | HOH739 |
| A | HOH749 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 612 |
| Chain | Residue |
| A | ASP13 |
| A | ASP254 |
| A | ASP258 |
| A | HOH775 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DIU B 601 |
| Chain | Residue |
| B | TYR149 |
| B | ARG198 |
| B | ARG217 |
| B | HIS241 |
| B | ARG256 |
| B | ALA260 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DIU B 602 |
| Chain | Residue |
| B | ILE387 |
| B | ASN390 |
| B | PHE402 |
| B | ARG409 |
| B | GLU449 |
| B | LEU452 |
| B | ARG484 |
| B | HOH746 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DIU B 603 |
| Chain | Residue |
| B | LEU115 |
| B | ILE181 |
| B | MET184 |
| B | ARG185 |
| B | PEG605 |
| B | HOH747 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DIU B 604 |
| Chain | Residue |
| B | LEU454 |
| B | ARG194 |
| B | LEU197 |
| B | ARG198 |
| B | SER201 |
| B | TRP213 |
| B | ARG217 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 605 |
| Chain | Residue |
| B | LEU115 |
| B | PHE133 |
| B | LYS136 |
| B | TYR137 |
| B | TYR160 |
| B | DIU603 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE B 606 |
| Chain | Residue |
| B | PHE205 |
| B | ARG208 |
| B | GLY327 |
| B | LEU346 |
| B | HOH733 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE B 607 |
| Chain | Residue |
| B | PHE506 |
| B | LYS524 |
| B | MET547 |
| B | PHE550 |
| B | LEU574 |
| B | THR578 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA B 608 |
| Chain | Residue |
| B | SER109 |
| B | HOH717 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 609 |
| Chain | Residue |
| B | GLU243 |
| B | ASP248 |
| B | GLU251 |
| B | HOH748 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 610 |
| Chain | Residue |
| B | ASP13 |
| B | ASP254 |
| B | ASP258 |
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 |
