4BCA
MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: Tyr578Phe mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005778 | cellular_component | peroxisomal membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008609 | molecular_function | alkylglycerone-phosphate synthase activity |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0008611 | biological_process | ether lipid biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005778 | cellular_component | peroxisomal membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008609 | molecular_function | alkylglycerone-phosphate synthase activity |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0008611 | biological_process | ether lipid biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005778 | cellular_component | peroxisomal membrane |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0008609 | molecular_function | alkylglycerone-phosphate synthase activity |
| C | 0008610 | biological_process | lipid biosynthetic process |
| C | 0008611 | biological_process | ether lipid biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016740 | molecular_function | transferase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005777 | cellular_component | peroxisome |
| D | 0005778 | cellular_component | peroxisomal membrane |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0008609 | molecular_function | alkylglycerone-phosphate synthase activity |
| D | 0008610 | biological_process | lipid biosynthetic process |
| D | 0008611 | biological_process | ether lipid biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016740 | molecular_function | transferase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD A 999 |
| Chain | Residue |
| A | TRP96 |
| A | GLY244 |
| A | PRO302 |
| A | ASP303 |
| A | SER304 |
| A | SER308 |
| A | THR309 |
| A | GLY312 |
| A | TRP313 |
| A | SER315 |
| A | THR316 |
| A | PRO234 |
| A | ALA318 |
| A | SER319 |
| A | GLU368 |
| A | GLY369 |
| A | GLY372 |
| A | VAL373 |
| A | ILE374 |
| A | ALA512 |
| A | HIS616 |
| A | ASN654 |
| A | ILE235 |
| A | ASN656 |
| A | CL1659 |
| A | HOH2040 |
| A | HOH2055 |
| A | HOH2056 |
| A | HOH2060 |
| A | HOH2084 |
| A | GLY236 |
| A | GLY237 |
| A | GLY238 |
| A | THR239 |
| A | SER240 |
| A | VAL241 |
| site_id | AC2 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD B 999 |
| Chain | Residue |
| B | TRP96 |
| B | PRO234 |
| B | ILE235 |
| B | GLY236 |
| B | GLY237 |
| B | GLY238 |
| B | THR239 |
| B | SER240 |
| B | VAL241 |
| B | GLY244 |
| B | LEU245 |
| B | PRO302 |
| B | ASP303 |
| B | SER304 |
| B | SER308 |
| B | THR309 |
| B | GLY311 |
| B | GLY312 |
| B | TRP313 |
| B | SER315 |
| B | THR316 |
| B | ALA318 |
| B | SER319 |
| B | GLU368 |
| B | GLY369 |
| B | GLY372 |
| B | VAL373 |
| B | ILE374 |
| B | ALA512 |
| B | HIS616 |
| B | ASN654 |
| B | ASN656 |
| B | CL1659 |
| B | HOH2030 |
| B | HOH2031 |
| B | HOH2033 |
| B | HOH2049 |
| B | HOH2050 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD C 999 |
| Chain | Residue |
| C | VAL373 |
| C | ILE374 |
| C | ALA512 |
| C | HIS616 |
| C | ASN656 |
| C | CL1659 |
| C | HOH2046 |
| C | HOH2049 |
| C | HOH2062 |
| C | HOH2065 |
| C | TRP96 |
| C | PRO234 |
| C | ILE235 |
| C | GLY236 |
| C | GLY237 |
| C | GLY238 |
| C | THR239 |
| C | SER240 |
| C | GLY244 |
| C | LEU245 |
| C | PRO302 |
| C | ASP303 |
| C | SER304 |
| C | SER308 |
| C | THR309 |
| C | GLY311 |
| C | GLY312 |
| C | TRP313 |
| C | SER315 |
| C | THR316 |
| C | ALA318 |
| C | SER319 |
| C | GLU368 |
| C | GLY369 |
| C | GLY372 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD D 999 |
| Chain | Residue |
| D | TRP96 |
| D | PRO234 |
| D | ILE235 |
| D | GLY236 |
| D | GLY237 |
| D | GLY238 |
| D | THR239 |
| D | SER240 |
| D | GLY244 |
| D | LEU245 |
| D | PRO302 |
| D | ASP303 |
| D | SER304 |
| D | SER308 |
| D | THR309 |
| D | GLY311 |
| D | GLY312 |
| D | TRP313 |
| D | SER315 |
| D | THR316 |
| D | ALA318 |
| D | SER319 |
| D | GLU368 |
| D | GLY369 |
| D | GLY372 |
| D | VAL373 |
| D | ILE374 |
| D | ALA512 |
| D | HIS616 |
| D | ASN656 |
| D | CL1659 |
| D | HOH2045 |
| D | HOH2048 |
| D | HOH2062 |
| D | HOH2063 |
| D | HOH2065 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1659 |
| Chain | Residue |
| A | PHE578 |
| A | HIS617 |
| A | FAD999 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1659 |
| Chain | Residue |
| B | PHE578 |
| B | HIS617 |
| B | FAD999 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 1659 |
| Chain | Residue |
| D | PHE578 |
| D | HIS617 |
| D | FAD999 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 1659 |
| Chain | Residue |
| C | HIS617 |
| C | FAD999 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1660 |
| Chain | Residue |
| A | TYR571 |
| A | ASP572 |
| A | HOH2065 |
| A | HOH2125 |
| B | LYS380 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1661 |
| Chain | Residue |
| A | ILE325 |
| A | PRO415 |
| A | ALA416 |
| A | PHE470 |
| A | GLU471 |
| A | HIS480 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1660 |
| Chain | Residue |
| D | ILE325 |
| D | PRO415 |
| D | ALA416 |
| D | PHE470 |
| D | GLU471 |
| D | HIS480 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1660 |
| Chain | Residue |
| C | PRO415 |
| C | ALA416 |
| C | PHE470 |
| C | GLU471 |
| C | HIS480 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1661 |
| Chain | Residue |
| C | LYS380 |
| D | ASP572 |
| D | HOH2067 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1660 |
| Chain | Residue |
| B | ILE325 |
| B | ALA414 |
| B | PRO415 |
| B | ALA416 |
| B | PHE470 |
| B | GLU471 |
| B | HIS480 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1661 |
| Chain | Residue |
| B | LYS323 |
| B | TYR571 |
| B | ASP572 |
| B | HOH2053 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:23112191 |
| Chain | Residue | Details |
| A | PHE578 | |
| B | PHE578 | |
| C | PHE578 | |
| D | PHE578 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23112191 |
| Chain | Residue | Details |
| A | PRO234 | |
| B | ARG515 | |
| C | PRO234 | |
| C | ASP303 | |
| C | THR316 | |
| C | GLU368 | |
| C | ARG515 | |
| D | PRO234 | |
| D | ASP303 | |
| D | THR316 | |
| D | GLU368 | |
| A | ASP303 | |
| D | ARG515 | |
| A | THR316 | |
| A | GLU368 | |
| A | ARG515 | |
| B | PRO234 | |
| B | ASP303 | |
| B | THR316 | |
| B | GLU368 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Important for enzyme activity => ECO:0000269|PubMed:10692424, ECO:0000269|PubMed:23112191 |
| Chain | Residue | Details |
| A | ARG419 | |
| B | ARG419 | |
| C | ARG419 | |
| D | ARG419 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O00116 |
| Chain | Residue | Details |
| A | SER65 | |
| B | SER65 | |
| C | SER65 | |
| D | SER65 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O00116 |
| Chain | Residue | Details |
| A | THR74 | |
| B | THR74 | |
| C | THR74 | |
| D | THR74 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O00116 |
| Chain | Residue | Details |
| A | LYS102 | |
| A | LYS347 | |
| B | LYS102 | |
| B | LYS347 | |
| C | LYS102 | |
| C | LYS347 | |
| D | LYS102 | |
| D | LYS347 |
