3M4Z
Crystal Structure of B. subtilis ferrochelatase with Cobalt 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 CO A 310 |
| Chain | Residue |
| A | HIS182 |
| A | GLU263 |
| A | HOH460 |
| A | HOH514 |
| A | HOH531 |
| A | HOH532 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 311 |
| Chain | Residue |
| A | HOH511 |
| A | HOH512 |
| A | HOH513 |
| A | HOH424 |
| A | HOH509 |
| A | HOH510 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 312 |
| Chain | Residue |
| A | HOH394 |
| A | HOH453 |
| A | HOH456 |
| A | HOH459 |
| A | HOH534 |
| A | HOH535 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 313 |
| Chain | Residue |
| A | GLU19 |
| A | HOH536 |
| A | HOH537 |
| A | HOH538 |
| A | HOH539 |
| A | HOH540 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 314 |
| Chain | Residue |
| A | ARG32 |
| A | SER145 |
| A | GLN198 |
| A | HOH512 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 315 |
| Chain | Residue |
| A | GLU144 |
| A | LYS306 |
Functional Information from PROSITE/UniProt
| site_id | PS00534 |
| Number of Residues | 19 |
| Details | FERROCHELATASE Ferrochelatase signature. LIvSaHSLPekik.EfGDp...Y |
| Chain | Residue | Details |
| A | LEU177-TYR195 |
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 |
