4IFB
Crystal structure of SULT 2A1 LLGG mutant with PAPS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004027 | molecular_function | alcohol sulfotransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006068 | biological_process | ethanol catabolic process |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0008146 | molecular_function | sulfotransferase activity |
A | 0008202 | biological_process | steroid metabolic process |
A | 0008203 | biological_process | cholesterol metabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030573 | biological_process | bile acid catabolic process |
A | 0042403 | biological_process | thyroid hormone metabolic process |
A | 0047704 | molecular_function | bile-salt sulfotransferase activity |
A | 0050294 | molecular_function | steroid sulfotransferase activity |
A | 0050427 | biological_process | 3'-phosphoadenosine 5'-phosphosulfate metabolic process |
A | 0050656 | molecular_function | 3'-phosphoadenosine 5'-phosphosulfate binding |
A | 0051923 | biological_process | sulfation |
B | 0004027 | molecular_function | alcohol sulfotransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006068 | biological_process | ethanol catabolic process |
B | 0006805 | biological_process | xenobiotic metabolic process |
B | 0008146 | molecular_function | sulfotransferase activity |
B | 0008202 | biological_process | steroid metabolic process |
B | 0008203 | biological_process | cholesterol metabolic process |
B | 0016042 | biological_process | lipid catabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0030573 | biological_process | bile acid catabolic process |
B | 0042403 | biological_process | thyroid hormone metabolic process |
B | 0047704 | molecular_function | bile-salt sulfotransferase activity |
B | 0050294 | molecular_function | steroid sulfotransferase activity |
B | 0050427 | biological_process | 3'-phosphoadenosine 5'-phosphosulfate metabolic process |
B | 0050656 | molecular_function | 3'-phosphoadenosine 5'-phosphosulfate binding |
B | 0051923 | biological_process | sulfation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 A 301 |
Chain | Residue |
A | LYS248 |
A | ASP253 |
A | HIS257 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE PPS A 302 |
Chain | Residue |
A | TRP49 |
A | HIS99 |
A | ARG121 |
A | SER129 |
A | TYR184 |
A | SER218 |
A | SER219 |
A | PHE220 |
A | MET223 |
A | LEU245 |
A | LEU246 |
A | ARG247 |
A | LYS248 |
A | GLY249 |
A | HOH402 |
A | HOH403 |
A | HOH422 |
A | HOH438 |
A | HOH503 |
A | PRO43 |
A | LYS44 |
A | SER45 |
A | GLY46 |
A | THR47 |
A | ASN48 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 303 |
Chain | Residue |
A | ARG174 |
A | GLU176 |
A | PHE179 |
A | HOH496 |
A | HOH497 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 301 |
Chain | Residue |
B | LYS248 |
B | ASP253 |
B | ASN256 |
B | HIS257 |
site_id | AC5 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE PPS B 302 |
Chain | Residue |
B | PRO43 |
B | LYS44 |
B | SER45 |
B | GLY46 |
B | THR47 |
B | ASN48 |
B | TRP49 |
B | HIS99 |
B | ARG121 |
B | SER129 |
B | TYR184 |
B | SER218 |
B | SER219 |
B | PHE220 |
B | MET223 |
B | LEU245 |
B | LEU246 |
B | ARG247 |
B | LYS248 |
B | GLY249 |
B | HOH403 |
B | HOH427 |
B | HOH432 |
B | HOH449 |
B | HOH493 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 303 |
Chain | Residue |
B | HIS58 |
B | LYS60 |
B | LYS204 |
B | HOH477 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K B 304 |
Chain | Residue |
B | ARG174 |
B | GLU176 |
B | PHE179 |
B | HOH418 |
B | HOH483 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 305 |
Chain | Residue |
B | TYR131 |
B | PHE132 |
B | HIS257 |
B | HOH410 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11988089, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1J99, ECO:0007744|PDB:1OV4 |
Chain | Residue | Details |
A | HIS99 | |
B | HIS99 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10854859, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:1OV4, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB |
Chain | Residue | Details |
A | LYS44 | |
A | GLY46 | |
A | ASN48 | |
B | LYS44 | |
B | GLY46 | |
B | ASN48 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB |
Chain | Residue | Details |
A | SER45 | |
B | SER45 | |
B | THR47 | |
B | TRP49 | |
B | ARG121 | |
B | SER129 | |
B | SER218 | |
B | ARG247 | |
B | LYS248 | |
B | GLY249 | |
A | THR47 | |
A | TRP49 | |
A | ARG121 | |
A | SER129 | |
A | SER218 | |
A | ARG247 | |
A | LYS248 | |
A | GLY249 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:4IFB |
Chain | Residue | Details |
A | TYR184 | |
B | TYR184 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:4IFB |
Chain | Residue | Details |
A | MET223 | |
B | MET223 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER251 | |
B | SER251 |