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Literature summary extracted from
- Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis (1997), Structure, 5, 1501-1510.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.99.1.9 | the three-dimensional structure is determined at 1.9 A resolution by the method of multiple isomorphous replacement. The structural model contains 308 of the 310 amino acid residues of the protein and 198 solvent molecules | Bacillus subtilis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.99.1.9 | Bacillus subtilis | - |
- |
- |
| 4.99.1.9 | Bacillus subtilis 168 | - |
- |
- |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.99.1.9 | metabolism | the enzyme catalyzes the terminal step in heme biosynthesis | Bacillus subtilis |
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