2Q2N
Crystal structure of Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride
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 1000 |
| Chain | Residue |
| A | HOH9002 |
| A | HOH9003 |
| A | HOH9004 |
| A | HOH9005 |
| A | HOH9006 |
| A | HOH9007 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 2000 |
| Chain | Residue |
| A | HOH9011 |
| A | HOH9012 |
| A | HOH9013 |
| A | HOH9008 |
| A | HOH9009 |
| A | HOH9010 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE H01 A 9001 |
| Chain | Residue |
| A | TYR13 |
| A | ILE29 |
| A | ARG30 |
| A | ARG31 |
| A | ARG33 |
| A | MET39 |
| A | PHE120 |
| A | HIS183 |
| A | SER184 |
| A | LEU185 |
| A | PRO195 |
| A | GLN199 |
| A | GLY224 |
| A | ASN225 |
| A | THR226 |
| A | PRO227 |
| A | TRP230 |
| A | HOH9032 |
| A | HOH9068 |
| A | HOH9093 |
| A | HOH9127 |
| A | HOH9181 |
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 |
