4ZAC
Structure of S. cerevisiae Fdc1 with the prenylated-flavin cofactor 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 | 6 |
| Details | binding site for residue NA A 601 |
| Chain | Residue |
| A | ASP62 |
| A | ASP310 |
| A | HOH958 |
| A | HOH1040 |
| A | HOH1061 |
| A | HOH1067 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 602 |
| Chain | Residue |
| A | MET228 |
| A | GLU236 |
| A | 4LU604 |
| A | TRP171 |
| A | VAL225 |
| A | SER226 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 603 |
| Chain | Residue |
| A | ASN170 |
| A | HIS193 |
| A | GLU236 |
| A | 4LU604 |
| A | HOH774 |
| A | HOH867 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | binding site for residue 4LU A 604 |
| Chain | Residue |
| A | THR155 |
| A | ASN170 |
| A | SER172 |
| A | ILE173 |
| A | ALA174 |
| A | ARG175 |
| A | LEU187 |
| A | GLN192 |
| A | HIS193 |
| A | SER226 |
| A | SER227 |
| A | MET228 |
| A | PRO229 |
| A | GLU236 |
| A | SER317 |
| A | PRO319 |
| A | ILE330 |
| A | LYS394 |
| A | K602 |
| A | MN603 |
| A | HOH722 |
| A | HOH744 |
| A | HOH774 |
| A | HOH775 |
| A | HOH943 |
| A | HOH982 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 601 |
| Chain | Residue |
| B | ASP62 |
| B | ASP310 |
| B | HOH939 |
| B | HOH949 |
| B | HOH1004 |
| B | HOH1015 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue K B 602 |
| Chain | Residue |
| B | TRP171 |
| B | VAL225 |
| B | SER226 |
| B | MET228 |
| B | GLU236 |
| B | 4LU604 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 603 |
| Chain | Residue |
| B | ASN170 |
| B | HIS193 |
| B | GLU236 |
| B | 4LU604 |
| B | HOH747 |
| B | HOH788 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | binding site for residue 4LU B 604 |
| Chain | Residue |
| B | THR155 |
| B | ASN170 |
| B | SER172 |
| B | ILE173 |
| B | ALA174 |
| B | ARG175 |
| B | LEU187 |
| B | GLN192 |
| B | HIS193 |
| B | SER226 |
| B | SER227 |
| B | MET228 |
| B | PRO229 |
| B | GLU236 |
| B | GLU285 |
| B | SER317 |
| B | PRO319 |
| B | ILE330 |
| B | LYS394 |
| B | K602 |
| B | MN603 |
| B | HOH747 |
| B | HOH769 |
| B | HOH814 |
| B | HOH860 |
| B | HOH941 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 601 |
| Chain | Residue |
| C | ASN170 |
| C | HIS193 |
| C | GLU236 |
| C | 4LU603 |
| C | HOH715 |
| C | HOH867 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue K C 602 |
| Chain | Residue |
| C | 4LU603 |
| C | TRP171 |
| C | VAL225 |
| C | SER226 |
| C | MET228 |
| C | GLU236 |
| site_id | AD2 |
| Number of Residues | 26 |
| Details | binding site for residue 4LU C 603 |
| Chain | Residue |
| C | THR155 |
| C | ASN170 |
| C | SER172 |
| C | ILE173 |
| C | ALA174 |
| C | ARG175 |
| C | LEU187 |
| C | GLN192 |
| C | HIS193 |
| C | SER226 |
| C | SER227 |
| C | MET228 |
| C | PRO229 |
| C | GLU236 |
| C | GLU285 |
| C | PRO319 |
| C | ILE330 |
| C | LYS394 |
| C | MN601 |
| C | K602 |
| C | HOH710 |
| C | HOH715 |
| C | HOH768 |
| C | HOH779 |
| C | HOH810 |
| C | HOH899 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue NA C 604 |
| Chain | Residue |
| C | ASP62 |
| C | ASP310 |
| C | HOH863 |
| C | HOH928 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MN D 601 |
| Chain | Residue |
| D | ASN170 |
| D | HIS193 |
| D | GLU236 |
| D | 4LU603 |
| D | HOH753 |
| D | HOH770 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue K D 602 |
| Chain | Residue |
| D | TRP171 |
| D | VAL225 |
| D | SER226 |
| D | MET228 |
| D | GLU236 |
| D | 4LU603 |
| site_id | AD6 |
| Number of Residues | 27 |
| Details | binding site for residue 4LU D 603 |
| Chain | Residue |
| D | THR155 |
| D | ASN170 |
| D | SER172 |
| D | ILE173 |
| D | ALA174 |
| D | ARG175 |
| D | LEU187 |
| D | GLN192 |
| D | HIS193 |
| D | SER226 |
| D | SER227 |
| D | MET228 |
| D | PRO229 |
| D | GLU236 |
| D | GLU285 |
| D | SER317 |
| D | PRO319 |
| D | ILE330 |
| D | LYS394 |
| D | MN601 |
| D | K602 |
| D | HOH750 |
| D | HOH753 |
| D | HOH772 |
| D | HOH812 |
| D | HOH823 |
| D | HOH920 |
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 |
| C | HIS193 | |
| C | GLU236 | |
| C | LYS394 | |
| D | ASN170 | |
| D | GLN192 | |
| D | HIS193 | |
| D | GLU236 | |
| D | LYS394 | |
| A | GLN192 | |
| A | ASN170 | |
| A | HIS193 | |
| A | GLU236 | |
| A | LYS394 | |
| B | ASN170 | |
| B | GLN192 | |
| B | HIS193 | |
| B | GLU236 | |
| B | LYS394 | |
| C | ASN170 | |
| C | GLN192 |
