Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004325 | molecular_function | ferrochelatase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
A | 0006783 | biological_process | heme biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 900 |
Chain | Residue |
A | HOH1202 |
A | HOH1203 |
A | HOH1204 |
A | HOH1205 |
A | HOH1206 |
A | HOH1207 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 901 |
Chain | Residue |
A | HOH1211 |
A | HOH1212 |
A | HOH1213 |
A | HOH1208 |
A | HOH1209 |
A | HOH1210 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 902 |
Chain | Residue |
A | GLU20 |
A | HOH1214 |
A | HOH1215 |
A | HOH1216 |
A | HOH1217 |
A | HOH1218 |
Functional Information from PROSITE/UniProt
site_id | PS00534 |
Number of Residues | 19 |
Details | FERROCHELATASE Ferrochelatase signature. LIvSaHSLPekik.EfGDp...Y |
Chain | Residue | Details |
A | LEU178-TYR196 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | TYR13 | |
A | ARG31 | |
A | HIS183 | |
A | LYS188 | |
Chain | Residue | Details |
A | GLU20 | |
Chain | Residue | Details |
A | ARG30 | |
A | SER54 | |
A | TYR125 | |
Chain | Residue | Details |
A | ARG46 | |
A | ASP268 | |
A | GLU272 | |
Chain | Residue | Details |
A | GLU264 | |