4ZR8
Structure of uroporphyrinogen decarboxylase from Acinetobacter baumannii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004853 | molecular_function | uroporphyrinogen decarboxylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006778 | biological_process | porphyrin-containing compound metabolic process |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019353 | biological_process | protoporphyrinogen IX biosynthetic process from glutamate |
| B | 0004853 | molecular_function | uroporphyrinogen decarboxylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006778 | biological_process | porphyrin-containing compound metabolic process |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019353 | biological_process | protoporphyrinogen IX biosynthetic process from glutamate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | HOH514 |
| A | HOH528 |
| A | HOH642 |
| A | HOH851 |
| B | HOH777 |
| B | HOH841 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | HOH634 |
| A | ASN225 |
| A | TYR226 |
| A | HOH585 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ARG27 |
| A | ILE78 |
| A | PHE207 |
| A | CL404 |
| A | HOH603 |
| A | HOH606 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | MET26 |
| A | ARG27 |
| A | EDO403 |
| A | HOH846 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ARG165 |
| A | GLN169 |
| B | TYR298 |
| B | TRP335 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 401 |
| Chain | Residue |
| A | TYR298 |
| A | TRP335 |
| B | ARG165 |
| B | GLN169 |
| B | HOH528 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | ASN225 |
| B | TYR226 |
| B | HOH579 |
| B | HOH684 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | ARG27 |
| B | ILE78 |
| B | PHE207 |
| B | CL404 |
| B | HOH510 |
| B | HOH642 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 404 |
| Chain | Residue |
| B | MET26 |
| B | ARG27 |
| B | EDO403 |
| B | HOH805 |
Functional Information from PROSITE/UniProt
