6EVE
Structure of R175A S. cerevisiae Fdc1 with prFMN in the iminium form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0033494 | biological_process | ferulate metabolic process |
| A | 0046281 | biological_process | cinnamic acid catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1901067 | biological_process | ferulate catabolic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0033494 | biological_process | ferulate metabolic process |
| B | 0046281 | biological_process | cinnamic acid catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1901067 | biological_process | ferulate catabolic process |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0033494 | biological_process | ferulate metabolic process |
| C | 0046281 | biological_process | cinnamic acid catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1901067 | biological_process | ferulate catabolic process |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0033494 | biological_process | ferulate metabolic process |
| D | 0046281 | biological_process | cinnamic acid catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1901067 | biological_process | ferulate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue 4LU A 601 |
| Chain | Residue |
| A | THR155 |
| A | SER227 |
| A | MET228 |
| A | PRO229 |
| A | GLU236 |
| A | SER317 |
| A | PRO319 |
| A | ILE330 |
| A | LYS394 |
| A | MN602 |
| A | K603 |
| A | ASN170 |
| A | HOH734 |
| A | HOH780 |
| A | HOH834 |
| A | HOH897 |
| A | SER172 |
| A | ILE173 |
| A | ALA174 |
| A | ALA175 |
| A | GLN192 |
| A | HIS193 |
| A | SER226 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 602 |
| Chain | Residue |
| A | ASN170 |
| A | HIS193 |
| A | GLU236 |
| A | 4LU601 |
| A | HOH780 |
| A | HOH859 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue K A 603 |
| Chain | Residue |
| A | TRP171 |
| A | VAL225 |
| A | SER226 |
| A | MET228 |
| A | GLU236 |
| A | 4LU601 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue 4LU B 601 |
| Chain | Residue |
| B | THR155 |
| B | ASN170 |
| B | SER172 |
| B | ILE173 |
| B | ALA174 |
| B | ALA175 |
| B | GLN192 |
| B | HIS193 |
| B | SER226 |
| B | SER227 |
| B | MET228 |
| B | PRO229 |
| B | GLU236 |
| B | PRO319 |
| B | ILE330 |
| B | LYS394 |
| B | MN602 |
| B | K603 |
| B | HOH717 |
| B | HOH754 |
| B | HOH808 |
| B | HOH842 |
| B | HOH883 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 602 |
| Chain | Residue |
| B | ASN170 |
| B | HIS193 |
| B | GLU236 |
| B | 4LU601 |
| B | HOH717 |
| B | HOH846 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue K B 603 |
| Chain | Residue |
| B | TRP171 |
| B | VAL225 |
| B | SER226 |
| B | MET228 |
| B | GLU236 |
| B | 4LU601 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | binding site for residue 4LU C 601 |
| Chain | Residue |
| C | THR155 |
| C | ASN170 |
| C | SER172 |
| C | ILE173 |
| C | ALA174 |
| C | ALA175 |
| C | GLN192 |
| C | HIS193 |
| C | SER226 |
| C | SER227 |
| C | MET228 |
| C | PRO229 |
| C | GLU236 |
| C | SER317 |
| C | PRO319 |
| C | ILE330 |
| C | LYS394 |
| C | MN602 |
| C | K603 |
| C | HOH722 |
| C | HOH772 |
| C | HOH781 |
| C | HOH868 |
| C | HOH925 |
| C | HOH943 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 602 |
| Chain | Residue |
| C | HOH722 |
| C | HOH906 |
| C | ASN170 |
| C | HIS193 |
| C | GLU236 |
| C | 4LU601 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue K C 603 |
| Chain | Residue |
| C | TRP171 |
| C | VAL225 |
| C | SER226 |
| C | MET228 |
| C | GLU236 |
| C | 4LU601 |
| site_id | AD1 |
| Number of Residues | 23 |
| Details | binding site for residue 4LU D 601 |
| Chain | Residue |
| D | THR155 |
| D | ASN170 |
| D | SER172 |
| D | ILE173 |
| D | ALA174 |
| D | ALA175 |
| D | GLN192 |
| D | HIS193 |
| D | SER226 |
| D | SER227 |
| D | MET228 |
| D | PRO229 |
| D | GLU236 |
| D | SER317 |
| D | PRO319 |
| D | ILE330 |
| D | LYS394 |
| D | MN602 |
| D | MN603 |
| D | HOH719 |
| D | HOH737 |
| D | HOH863 |
| D | HOH878 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MN D 602 |
| Chain | Residue |
| D | ASN170 |
| D | HIS193 |
| D | GLU236 |
| D | 4LU601 |
| D | HOH737 |
| D | HOH894 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MN D 603 |
| Chain | Residue |
| D | TRP171 |
| D | VAL225 |
| D | SER226 |
| D | MET228 |
| D | GLU236 |
| D | 4LU601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:A2QHE5, ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000305|PubMed:25862228 |
| Chain | Residue | Details |
| A | GLU285 | |
| B | GLU285 | |
| C | GLU285 | |
| D | GLU285 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754 |
| Chain | Residue | Details |
| A | ASN170 | |
| B | LYS394 | |
| C | ASN170 | |
| C | GLN192 | |
| C | HIS193 | |
| C | GLU236 | |
| C | LYS394 | |
| D | ASN170 | |
| D | GLN192 | |
| D | HIS193 | |
| D | GLU236 | |
| A | GLN192 | |
| D | LYS394 | |
| A | HIS193 | |
| A | GLU236 | |
| A | LYS394 | |
| B | ASN170 | |
| B | GLN192 | |
| B | HIS193 | |
| B | GLU236 |
