4BBY
MAMMALIAN ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE: WILD-TYPE
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 | 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 | 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 | 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 | 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 | 38 |
| Details | BINDING SITE FOR RESIDUE FAD A 999 |
| Chain | Residue |
| A | TRP96 |
| A | VAL241 |
| A | GLY244 |
| A | LEU245 |
| A | PRO302 |
| A | ASP303 |
| A | SER304 |
| A | SER308 |
| A | THR309 |
| A | GLY311 |
| A | GLY312 |
| A | HIS189 |
| A | TRP313 |
| A | SER315 |
| A | THR316 |
| A | ALA318 |
| A | SER319 |
| A | GLU368 |
| A | GLY369 |
| A | GLY372 |
| A | VAL373 |
| A | ILE374 |
| A | PRO234 |
| A | ALA512 |
| A | HIS616 |
| A | ASN654 |
| A | ASN656 |
| A | HOH2067 |
| A | HOH2069 |
| A | HOH2074 |
| A | HOH2106 |
| A | HOH2113 |
| A | ILE235 |
| A | GLY236 |
| A | GLY237 |
| A | GLY238 |
| A | THR239 |
| A | SER240 |
| site_id | AC2 |
| Number of Residues | 36 |
| 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 | 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 | HOH2056 |
| B | HOH2063 |
| B | HOH2085 |
| B | HOH2087 |
| B | HOH2111 |
| site_id | AC3 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD C 999 |
| Chain | Residue |
| C | GLY369 |
| C | GLY372 |
| C | VAL373 |
| C | ILE374 |
| C | ALA512 |
| C | HIS616 |
| C | ASN654 |
| C | ASN656 |
| C | HOH2071 |
| C | HOH2078 |
| C | HOH2100 |
| C | HOH2106 |
| C | TRP96 |
| C | HIS189 |
| C | PRO234 |
| C | ILE235 |
| C | GLY236 |
| C | GLY237 |
| C | GLY238 |
| C | THR239 |
| C | SER240 |
| C | VAL241 |
| C | GLY244 |
| C | LEU245 |
| C | THR260 |
| C | PRO302 |
| C | ASP303 |
| C | SER304 |
| C | SER308 |
| C | THR309 |
| C | GLY312 |
| C | TRP313 |
| C | SER315 |
| C | THR316 |
| C | ALA318 |
| C | SER319 |
| C | GLU368 |
| site_id | AC4 |
| Number of Residues | 35 |
| 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 | 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 | ASN654 |
| D | ASN656 |
| D | HOH2072 |
| D | HOH2077 |
| D | HOH2096 |
| D | HOH2097 |
| D | HOH2099 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1659 |
| Chain | Residue |
| C | LYS380 |
| D | LYS323 |
| D | TYR571 |
| D | ASP572 |
| D | HOH2103 |
| D | HOH2151 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1659 |
| Chain | Residue |
| A | LYS323 |
| A | TYR571 |
| A | ASP572 |
| A | HOH2116 |
| A | HOH2199 |
| B | LYS380 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1660 |
| Chain | Residue |
| A | GLY391 |
| A | SER392 |
| A | TYR485 |
| A | GLY497 |
| A | GLU498 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1659 |
| Chain | Residue |
| A | LYS380 |
| B | LYS323 |
| B | TYR571 |
| B | ASP572 |
| B | HOH2090 |
| B | HOH2157 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 728 |
| Details | Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Region: {"description":"Important for enzyme activity","evidences":[{"source":"PubMed","id":"10692424","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9989261","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Region: {"description":"Important for enzyme activity","evidences":[{"source":"PubMed","id":"9989261","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"23112191","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 88 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23112191","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for enzyme activity","evidences":[{"source":"PubMed","id":"10692424","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23112191","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O00116","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
