1C9E
STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE
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 | HOH652 |
| A | HOH653 |
| A | HOH654 |
| A | HOH655 |
| A | HOH656 |
| A | HOH657 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MP1 A 800 |
| Chain | Residue |
| A | ARG31 |
| A | PHE120 |
| A | SER121 |
| A | HIS183 |
| A | LEU185 |
| A | PRO186 |
| A | LYS188 |
| A | SER222 |
| A | THR226 |
| A | GLU264 |
| A | HOH434 |
| A | HOH452 |
| A | HOH521 |
| A | TYR13 |
| A | TYR25 |
| A | ILE29 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10704318","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1C1H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17198378","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21052751","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00323","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12761666","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00323","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12761666","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16140324","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17198378","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21052751","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hrk |
| Chain | Residue | Details |
| A | GLU264 | |
| A | HIS262 | |
| A | HIS183 |
