CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.910 | Heme Oxygenase; Chain A |
|
1.20.910.10 | Heme oxygenase-like |
Domain Context
CATH Clusters
| Superfamily | Heme oxygenase-like |
| Functional Family | Heme oxygenase 1 |
Enzyme Information
| 1.14.14.18 |
Heme oxygenase (biliverdin-producing).
based on mapping to UniProt P09601
Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O.
-!- This mammalian enzyme participates in the degradation of heme. -!- The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. -!- The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. -!- The enzyme requires NAD(P)H and EC 1.6.2.4. -!- Cf. EC 1.14.15.20. -!- Formerly EC 1.14.99.3.
|
UniProtKB Entries (1)
| P09601 |
HMOX1_HUMAN
Homo sapiens
Heme oxygenase 1
|
PDB Structure
| PDB | 3K4F |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Heme Oxygenase Inhibition by 2-Oxy-substituted 1-Azolyl-4-phenylbutanes: Effect of Variation of the Azole Moiety. X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 4-Phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone.
Chem.Biol.Drug Des.
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