1OLT
Coproporphyrinogen III oxidase (HemN) from Escherichia coli is a Radical SAM enzyme.
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | OXYGEN-INDEPENDENT COPROPORPHYRINOGEN III OXIDASE | polymer | 457 | 52781.8 | 1 | UniProt (P32131) Pfam (PF04055) Pfam (PF06969) | ESCHERICHIA COLI | COPROPORPHYRINOGENASE, COPROGEN OXIDASE |
| 2 | B (A) | IRON/SULFUR CLUSTER | non-polymer | 351.6 | 1 | Chemie (SF4) | |||
| 3 | C, D (A) | S-ADENOSYLMETHIONINE | non-polymer | 398.4 | 2 | Chemie (SAM) | |||
| 4 | E (A) | water | water | 18.0 | 396 | Chemie (HOH) |
Sequence modifications
A: 1 - 457 (UniProt: P32131)
| PDB | External Database | Details |
|---|---|---|
| Ser 386 | Ala 386 | conflict |
| Gln 390 | Lys 390 | conflict |
| Leu 395 | His 395 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 52781.8 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 1148.5 | |
| All* | Total formula weight | 53930.3 |
