5NCC
Structure of Fatty acid Photodecarboxylase in complex with FAD and palmitic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008812 | molecular_function | choline dehydrogenase activity |
| A | 0009507 | cellular_component | chloroplast |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0008812 | molecular_function | choline dehydrogenase activity |
| B | 0009507 | cellular_component | chloroplast |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0008812 | molecular_function | choline dehydrogenase activity |
| C | 0009507 | cellular_component | chloroplast |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0008812 | molecular_function | choline dehydrogenase activity |
| D | 0009507 | cellular_component | chloroplast |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0008812 | molecular_function | choline dehydrogenase activity |
| E | 0009507 | cellular_component | chloroplast |
| E | 0016020 | cellular_component | membrane |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| E | 0016829 | molecular_function | lyase activity |
| E | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0008812 | molecular_function | choline dehydrogenase activity |
| F | 0009507 | cellular_component | chloroplast |
| F | 0016020 | cellular_component | membrane |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| F | 0016829 | molecular_function | lyase activity |
| F | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | binding site for residue FAD A 701 |
| Chain | Residue |
| A | GLY90 |
| A | ALA158 |
| A | ARG159 |
| A | GLY160 |
| A | ARG161 |
| A | LEU162 |
| A | GLY165 |
| A | SER166 |
| A | SER167 |
| A | ASN170 |
| A | ALA171 |
| A | GLY92 |
| A | THR172 |
| A | LEU173 |
| A | ALA296 |
| A | VAL298 |
| A | CYS340 |
| A | ALA341 |
| A | GLY342 |
| A | HIS345 |
| A | LEU349 |
| A | ASN575 |
| A | THR93 |
| A | ASP609 |
| A | ALA610 |
| A | GLN620 |
| A | THR621 |
| A | GLY622 |
| A | VAL625 |
| A | PLM702 |
| A | ALA94 |
| A | LEU113 |
| A | GLU114 |
| A | ALA115 |
| A | PHE134 |
| A | TRP140 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue PLM A 702 |
| Chain | Residue |
| A | ALA171 |
| A | ARG451 |
| A | VAL453 |
| A | ALA457 |
| A | GLY462 |
| A | THR465 |
| A | TYR466 |
| A | PHE469 |
| A | THR484 |
| A | GLN486 |
| A | ASN575 |
| A | FAD701 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | binding site for residue FAD B 701 |
| Chain | Residue |
| B | GLY90 |
| B | GLY92 |
| B | THR93 |
| B | ALA94 |
| B | LEU113 |
| B | GLU114 |
| B | ALA115 |
| B | PHE134 |
| B | TRP140 |
| B | ALA158 |
| B | ARG159 |
| B | GLY160 |
| B | ARG161 |
| B | LEU162 |
| B | GLY165 |
| B | SER166 |
| B | SER167 |
| B | ASN170 |
| B | ALA171 |
| B | THR172 |
| B | LEU173 |
| B | ALA296 |
| B | VAL298 |
| B | CYS340 |
| B | ALA341 |
| B | GLY342 |
| B | HIS345 |
| B | LEU349 |
| B | ASN575 |
| B | ASP609 |
| B | ALA610 |
| B | GLN620 |
| B | THR621 |
| B | GLY622 |
| B | VAL625 |
| B | PLM702 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue PLM B 702 |
| Chain | Residue |
| B | ALA171 |
| B | ARG451 |
| B | VAL453 |
| B | MET456 |
| B | ALA457 |
| B | THR465 |
| B | TYR466 |
| B | GLN486 |
| B | ASN575 |
| B | FAD701 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | binding site for residue FAD C 701 |
| Chain | Residue |
| C | GLU114 |
| C | ALA115 |
| C | PHE134 |
| C | TRP140 |
| C | ALA158 |
| C | ARG159 |
| C | GLY160 |
| C | LEU162 |
| C | GLY165 |
| C | SER166 |
| C | SER167 |
| C | ASN170 |
| C | ALA171 |
| C | THR172 |
| C | LEU173 |
| C | ALA296 |
| C | ALA297 |
| C | VAL298 |
| C | CYS340 |
| C | ALA341 |
| C | GLY342 |
| C | HIS345 |
| C | ASN575 |
| C | ASP609 |
| C | ALA610 |
| C | GLN620 |
| C | THR621 |
| C | GLY622 |
| C | VAL625 |
| C | GLY90 |
| C | GLY92 |
| C | THR93 |
| C | ALA94 |
| C | LEU113 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue PLM C 702 |
| Chain | Residue |
| C | ALA171 |
| C | ARG451 |
| C | VAL453 |
| C | MET456 |
| C | ALA457 |
| C | GLY462 |
| C | THR465 |
| C | TYR466 |
| C | GLN486 |
| C | SER574 |
| C | ASN575 |
| site_id | AC7 |
| Number of Residues | 35 |
| Details | binding site for residue FAD D 701 |
| Chain | Residue |
| D | GLY90 |
| D | GLY92 |
| D | THR93 |
| D | ALA94 |
| D | LEU113 |
| D | GLU114 |
| D | ALA115 |
| D | PHE134 |
| D | TRP140 |
| D | ALA158 |
| D | ARG159 |
| D | GLY160 |
| D | LEU162 |
| D | GLY165 |
| D | SER166 |
| D | SER167 |
| D | ASN170 |
| D | ALA171 |
| D | THR172 |
| D | LEU173 |
| D | ALA296 |
| D | ALA297 |
| D | VAL298 |
| D | CYS340 |
| D | ALA341 |
| D | GLY342 |
| D | HIS345 |
| D | LEU349 |
| D | ASN575 |
| D | ASP609 |
| D | ALA610 |
| D | GLN620 |
| D | THR621 |
| D | GLY622 |
| D | VAL625 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue PLM D 702 |
| Chain | Residue |
| D | ARG451 |
| D | VAL453 |
| D | GLY462 |
| D | THR465 |
| D | TYR466 |
| D | THR484 |
| D | GLN486 |
| D | SER574 |
| D | ASN575 |
| site_id | AC9 |
| Number of Residues | 31 |
| Details | binding site for residue FAD E 701 |
| Chain | Residue |
| E | GLY90 |
| E | THR93 |
| E | LEU113 |
| E | GLU114 |
| E | ALA115 |
| E | PHE134 |
| E | TRP140 |
| E | ALA158 |
| E | ARG159 |
| E | GLY160 |
| E | LEU162 |
| E | GLY165 |
| E | SER166 |
| E | SER167 |
| E | ASN170 |
| E | ALA171 |
| E | THR172 |
| E | LEU173 |
| E | ALA296 |
| E | ALA297 |
| E | VAL298 |
| E | ALA341 |
| E | GLY342 |
| E | HIS345 |
| E | ASN575 |
| E | ASP609 |
| E | ALA610 |
| E | GLN620 |
| E | THR621 |
| E | GLY622 |
| E | VAL625 |
| site_id | AD1 |
| Number of Residues | 32 |
| Details | binding site for residue FAD F 701 |
| Chain | Residue |
| F | GLY90 |
| F | GLY92 |
| F | THR93 |
| F | ALA94 |
| F | LEU113 |
| F | GLU114 |
| F | PHE134 |
| F | TRP140 |
| F | ALA158 |
| F | GLY160 |
| F | ARG161 |
| F | LEU162 |
| F | GLY165 |
| F | SER166 |
| F | THR169 |
| F | ASN170 |
| F | ALA171 |
| F | THR172 |
| F | LEU173 |
| F | VAL298 |
| F | CYS340 |
| F | ALA341 |
| F | GLY342 |
| F | HIS345 |
| F | LEU349 |
| F | ASN575 |
| F | ASP609 |
| F | ALA610 |
| F | GLN620 |
| F | THR621 |
| F | GLY622 |
| F | VAL625 |
Functional Information from PROSITE/UniProt
| site_id | PS00624 |
| Number of Residues | 15 |
| Details | GMC_OXRED_2 GMC oxidoreductases signature 2. GAvhTPfLLkhSGVG |
| Chain | Residue | Details |
| A | GLY342-GLY356 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 78 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28860382","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NCC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






