6XUC
Structure of coproheme decarboxylase from Corynebacterium diphteriae in complex with coproheme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006785 | biological_process | heme B biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| A | 0020037 | molecular_function | heme binding |
| B | 0006785 | biological_process | heme B biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| B | 0020037 | molecular_function | heme binding |
| C | 0006785 | biological_process | heme B biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| C | 0020037 | molecular_function | heme binding |
| D | 0006785 | biological_process | heme B biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| D | 0020037 | molecular_function | heme binding |
| E | 0006785 | biological_process | heme B biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016634 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor |
| E | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue FEC A 401 |
| Chain | Residue |
| A | ASN115 |
| A | THR172 |
| A | TRP183 |
| A | LEU185 |
| A | PHE187 |
| A | MET199 |
| A | MET202 |
| A | ARG208 |
| A | HOH502 |
| A | HOH508 |
| A | HOH515 |
| A | HIS118 |
| A | HOH553 |
| A | HOH575 |
| A | TYR135 |
| A | PHE137 |
| A | ARG139 |
| A | TRP143 |
| A | HIS158 |
| A | ALA162 |
| A | ALA170 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue FEC B 301 |
| Chain | Residue |
| B | ASN115 |
| B | HIS118 |
| B | TYR135 |
| B | PHE137 |
| B | ARG139 |
| B | TRP143 |
| B | HIS158 |
| B | ALA162 |
| B | THR172 |
| B | LEU185 |
| B | PHE187 |
| B | MET199 |
| B | MET202 |
| B | ARG208 |
| B | HOH406 |
| B | HOH410 |
| B | HOH440 |
| B | HOH452 |
| B | HOH478 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue FEC C 401 |
| Chain | Residue |
| C | ASN115 |
| C | HIS118 |
| C | TYR135 |
| C | PHE137 |
| C | ARG139 |
| C | TRP143 |
| C | HIS158 |
| C | ALA162 |
| C | TRP183 |
| C | LEU185 |
| C | PHE187 |
| C | MET199 |
| C | MET202 |
| C | ARG208 |
| C | HOH503 |
| C | HOH506 |
| C | HOH518 |
| C | HOH538 |
| C | HOH559 |
| C | HOH578 |
| C | HOH587 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue FEC D 401 |
| Chain | Residue |
| D | ASN115 |
| D | HIS118 |
| D | TYR135 |
| D | PHE137 |
| D | ARG139 |
| D | TRP143 |
| D | HIS158 |
| D | ALA162 |
| D | ARG163 |
| D | PHE187 |
| D | MET199 |
| D | MET202 |
| D | ARG208 |
| D | HOH515 |
| D | HOH532 |
| D | HOH535 |
| D | HOH547 |
| D | HOH554 |
| D | HOH555 |
| D | HOH569 |
| D | HOH578 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue FEC E 401 |
| Chain | Residue |
| E | HOH519 |
| E | HOH560 |
| E | ASN115 |
| E | HIS118 |
| E | TYR135 |
| E | PHE137 |
| E | ARG139 |
| E | TRP143 |
| E | HIS158 |
| E | ALA162 |
| E | ALA170 |
| E | TRP183 |
| E | LEU185 |
| E | PHE187 |
| E | MET199 |
| E | MET202 |
| E | ARG208 |
| E | HOH510 |
| E | HOH511 |






