6R2R
Aspergillus niger ferulic acid decarboxylase (Fdc) in complex with prFMN (purified in dark) and alphafluorocinnamic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009074 | biological_process | aromatic amino acid family catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0018966 | biological_process | styrene metabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0033494 | biological_process | ferulate metabolic process |
| A | 0042537 | biological_process | benzene-containing compound metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046281 | biological_process | cinnamic acid catabolic process |
| A | 0046395 | biological_process | carboxylic acid catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120254 | biological_process | olefinic compound metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue MN A 601 |
| Chain | Residue |
| A | ASN168 |
| A | HIS191 |
| A | GLU233 |
| A | K602 |
| A | BYN604 |
| A | HOH752 |
| A | HOH839 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue K A 602 |
| Chain | Residue |
| A | SER223 |
| A | MET225 |
| A | GLU233 |
| A | MN601 |
| A | BYN604 |
| A | TRP169 |
| A | ALA222 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue K A 603 |
| Chain | Residue |
| A | ARG421 |
| A | ASP427 |
| A | ASP459 |
| A | LEU461 |
| A | HOH1080 |
| A | HOH1190 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | binding site for residue BYN A 604 |
| Chain | Residue |
| A | THR153 |
| A | ASN168 |
| A | SER170 |
| A | ILE171 |
| A | ALA172 |
| A | ARG173 |
| A | LEU185 |
| A | GLN190 |
| A | HIS191 |
| A | SER223 |
| A | SER224 |
| A | MET225 |
| A | PRO226 |
| A | GLU233 |
| A | GLU282 |
| A | ILE327 |
| A | LYS391 |
| A | MN601 |
| A | K602 |
| A | 4LW605 |
| A | HOH752 |
| A | HOH759 |
| A | HOH763 |
| A | HOH788 |
| A | HOH817 |
| A | HOH981 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue 4LW A 605 |
| Chain | Residue |
| A | ARG173 |
| A | GLN190 |
| A | GLU282 |
| A | MET283 |
| A | PHE437 |
| A | LEU439 |
| A | BYN604 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_03196","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26083754","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03196","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26083754","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03196","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
