6FXQ
Structure of coproheme decarboxylase from Listeria monocytogenes during turnover
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0006783 | biological_process | heme biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0006783 | biological_process | heme biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
| E | 0004601 | molecular_function | peroxidase activity |
| E | 0006783 | biological_process | heme biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 301 |
| Chain | Residue |
| A | ILE63 |
| A | LEU64 |
| A | GLY65 |
| A | ALA68 |
| A | ASP69 |
| A | HOH401 |
| B | GLU86 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue FEC A 302 |
| Chain | Residue |
| A | TYR147 |
| A | MET149 |
| A | LYS151 |
| A | HIS174 |
| A | GLY175 |
| A | GLY178 |
| A | ARG179 |
| A | GLN187 |
| A | TRP200 |
| A | LEU204 |
| A | ILE215 |
| A | MET219 |
| A | SER225 |
| A | PHE231 |
| A | VOV303 |
| A | HOH405 |
| A | HOH409 |
| A | HOH420 |
| A | HOH451 |
| D | HIS42 |
| A | SER111 |
| A | TYR113 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue VOV A 303 |
| Chain | Residue |
| A | LEU110 |
| A | SER111 |
| A | TYR113 |
| A | ARG133 |
| A | TYR147 |
| A | MET149 |
| A | LYS151 |
| A | TRP159 |
| A | HIS174 |
| A | GLY178 |
| A | ARG179 |
| A | VAL185 |
| A | GLN187 |
| A | TRP200 |
| A | LEU204 |
| A | ILE215 |
| A | MET219 |
| A | SER225 |
| A | PHE231 |
| A | FEC302 |
| A | HOH405 |
| A | HOH409 |
| A | HOH451 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MPD A 304 |
| Chain | Residue |
| A | GLU80 |
| A | ASN83 |
| A | ASN87 |
| C | SER62 |
| C | GLN244 |
| C | LYS247 |
| C | LEU248 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 301 |
| Chain | Residue |
| B | ILE63 |
| B | LEU64 |
| B | GLY65 |
| B | ALA68 |
| B | HOH410 |
| E | GLU86 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue FEC B 302 |
| Chain | Residue |
| B | TYR147 |
| B | MET149 |
| B | HIS174 |
| B | GLY178 |
| B | GLN187 |
| B | TRP200 |
| B | LEU204 |
| B | MET219 |
| B | SER225 |
| B | PHE231 |
| B | VOV303 |
| B | HOH402 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue VOV B 303 |
| Chain | Residue |
| B | LEU110 |
| B | SER111 |
| B | ARG133 |
| B | TYR147 |
| B | MET149 |
| B | TRP159 |
| B | HIS174 |
| B | GLY178 |
| B | GLN187 |
| B | TRP200 |
| B | VAL202 |
| B | LEU204 |
| B | MET219 |
| B | SER225 |
| B | PHE231 |
| B | FEC302 |
| B | HOH402 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 304 |
| Chain | Residue |
| A | LEU248 |
| B | GLU80 |
| B | ASN83 |
| B | ASN87 |
| B | HOH401 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 305 |
| Chain | Residue |
| A | GLU86 |
| C | ILE63 |
| C | LEU64 |
| C | GLY65 |
| C | ALA68 |
| C | HOH404 |
| site_id | AD1 |
| Number of Residues | 19 |
| Details | binding site for residue FEC C 301 |
| Chain | Residue |
| C | SER111 |
| C | TYR113 |
| C | ARG133 |
| C | TYR147 |
| C | MET149 |
| C | TRP159 |
| C | HIS174 |
| C | GLY178 |
| C | ARG179 |
| C | GLN187 |
| C | TRP200 |
| C | LEU204 |
| C | MET219 |
| C | SER225 |
| C | PHE231 |
| C | VOV302 |
| C | HOH402 |
| C | HOH408 |
| C | HOH456 |
| site_id | AD2 |
| Number of Residues | 20 |
| Details | binding site for residue VOV C 302 |
| Chain | Residue |
| C | LEU110 |
| C | SER111 |
| C | TYR113 |
| C | TYR147 |
| C | MET149 |
| C | TRP159 |
| C | HIS174 |
| C | GLY178 |
| C | ARG179 |
| C | VAL185 |
| C | GLN187 |
| C | TRP200 |
| C | LEU204 |
| C | ILE215 |
| C | MET219 |
| C | SER225 |
| C | PHE231 |
| C | FEC301 |
| C | HOH402 |
| C | HOH408 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 303 |
| Chain | Residue |
| C | GLU86 |
| D | ILE63 |
| D | LEU64 |
| D | GLY65 |
| D | ALA68 |
| D | HOH432 |
| site_id | AD4 |
| Number of Residues | 25 |
| Details | binding site for residue FEC D 301 |
| Chain | Residue |
| D | LEU110 |
| D | SER111 |
| D | TYR113 |
| D | ARG133 |
| D | TYR147 |
| D | MET149 |
| D | LYS151 |
| D | TRP159 |
| D | ILE171 |
| D | HIS174 |
| D | GLY178 |
| D | ARG179 |
| D | GLN187 |
| D | TRP200 |
| D | LEU204 |
| D | ILE215 |
| D | MET219 |
| D | SER225 |
| D | PHE231 |
| D | VOV302 |
| D | HOH402 |
| D | HOH412 |
| D | HOH465 |
| D | HOH474 |
| D | HOH481 |
| site_id | AD5 |
| Number of Residues | 23 |
| Details | binding site for residue VOV D 302 |
| Chain | Residue |
| D | GLU109 |
| D | SER111 |
| D | TYR113 |
| D | TYR147 |
| D | MET149 |
| D | LYS151 |
| D | TRP159 |
| D | HIS174 |
| D | GLY178 |
| D | ARG179 |
| D | VAL185 |
| D | GLN187 |
| D | TRP200 |
| D | LEU204 |
| D | ILE215 |
| D | MET219 |
| D | SER225 |
| D | PHE231 |
| D | FEC301 |
| D | HOH402 |
| D | HOH412 |
| D | HOH465 |
| D | HOH481 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue MPD D 303 |
| Chain | Residue |
| C | ASN87 |
| D | GLN244 |
| D | LYS247 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 304 |
| Chain | Residue |
| D | GLU86 |
| E | ILE63 |
| E | LEU64 |
| E | GLY65 |
| E | ALA68 |
| E | HOH412 |
| site_id | AD8 |
| Number of Residues | 16 |
| Details | binding site for residue FEC E 301 |
| Chain | Residue |
| E | SER111 |
| E | TYR113 |
| E | TYR147 |
| E | MET149 |
| E | TRP159 |
| E | HIS174 |
| E | GLY178 |
| E | ARG179 |
| E | GLN187 |
| E | TRP200 |
| E | LEU204 |
| E | MET219 |
| E | SER225 |
| E | VOV302 |
| E | HOH401 |
| E | HOH428 |
| site_id | AD9 |
| Number of Residues | 22 |
| Details | binding site for residue VOV E 302 |
| Chain | Residue |
| E | LEU110 |
| E | SER111 |
| E | TYR113 |
| E | ARG133 |
| E | TYR147 |
| E | MET149 |
| E | TRP159 |
| E | HIS174 |
| E | GLY178 |
| E | ARG179 |
| E | VAL185 |
| E | GLN187 |
| E | TRP200 |
| E | LEU204 |
| E | ILE215 |
| E | MET219 |
| E | SER225 |
| E | PHE231 |
| E | FEC301 |
| E | HOH401 |
| E | HOH428 |
| E | HOH464 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue MPD E 303 |
| Chain | Residue |
| B | GLN244 |
| E | GLU84 |
| E | ASN87 |
| E | HOH442 |
| E | HOH452 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:31423350 |
| Chain | Residue | Details |
| A | TYR147 | |
| B | TYR147 | |
| C | TYR147 | |
| D | TYR147 | |
| E | TYR147 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ |
| Chain | Residue | Details |
| B | TYR147 | |
| B | GLN187 | |
| B | SER225 | |
| C | ARG133 | |
| C | TYR147 | |
| C | GLN187 | |
| C | SER225 | |
| D | ARG133 | |
| D | TYR147 | |
| D | GLN187 | |
| D | SER225 | |
| E | ARG133 | |
| E | TYR147 | |
| E | GLN187 | |
| E | SER225 | |
| A | TYR147 | |
| A | GLN187 | |
| A | SER225 | |
| B | ARG133 | |
| A | ARG133 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ |
| Chain | Residue | Details |
| A | HIS174 | |
| B | HIS174 | |
| C | HIS174 | |
| D | HIS174 | |
| E | HIS174 |
