Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004325 | molecular_function | ferrochelatase activity |
A | 0005737 | cellular_component | cytoplasm |
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 400 |
Chain | Residue |
A | HOH311 |
A | HOH312 |
A | HOH313 |
A | HOH314 |
A | HOH315 |
A | HOH316 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | HOH320 |
A | HOH321 |
A | HOH322 |
A | HOH317 |
A | HOH318 |
A | HOH319 |
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 | MET13 | |
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 | |