5NCC
Structure of Fatty acid Photodecarboxylase in complex with FAD and palmitic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009507 | cellular_component | chloroplast |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0016829 | molecular_function | lyase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0009507 | cellular_component | chloroplast |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0016829 | molecular_function | lyase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0009507 | cellular_component | chloroplast |
C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
C | 0016829 | molecular_function | lyase activity |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0009507 | cellular_component | chloroplast |
D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
D | 0016829 | molecular_function | lyase activity |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0009507 | cellular_component | chloroplast |
E | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
E | 0016829 | molecular_function | lyase activity |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0009507 | cellular_component | chloroplast |
F | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
F | 0016829 | molecular_function | lyase activity |
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 | 66 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28860382, ECO:0007744|PDB:5NCC |
Chain | Residue | Details |
A | THR93 | |
A | GLN486 | |
A | GLY622 | |
B | THR93 | |
B | GLU114 | |
B | LEU162 | |
B | SER166 | |
B | ASN170 | |
B | VAL298 | |
B | CYS432 | |
B | ARG451 | |
A | GLU114 | |
B | TYR466 | |
B | GLN486 | |
B | GLY622 | |
C | THR93 | |
C | GLU114 | |
C | LEU162 | |
C | SER166 | |
C | ASN170 | |
C | VAL298 | |
C | CYS432 | |
A | LEU162 | |
C | ARG451 | |
C | TYR466 | |
C | GLN486 | |
C | GLY622 | |
D | THR93 | |
D | GLU114 | |
D | LEU162 | |
D | SER166 | |
D | ASN170 | |
D | VAL298 | |
A | SER166 | |
D | CYS432 | |
D | ARG451 | |
D | TYR466 | |
D | GLN486 | |
D | GLY622 | |
E | THR93 | |
E | GLU114 | |
E | LEU162 | |
E | SER166 | |
E | ASN170 | |
A | ASN170 | |
E | VAL298 | |
E | CYS432 | |
E | ARG451 | |
E | TYR466 | |
E | GLN486 | |
E | GLY622 | |
F | THR93 | |
F | GLU114 | |
F | LEU162 | |
F | SER166 | |
A | VAL298 | |
F | ASN170 | |
F | VAL298 | |
F | CYS432 | |
F | ARG451 | |
F | TYR466 | |
F | GLN486 | |
F | GLY622 | |
A | CYS432 | |
A | ARG451 | |
A | TYR466 |