First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
1n45
From Proteopedia
| 1n45, resolution 1.50Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||||
| Ligands: | , | ||||||||
| Gene: | HMOX1, HO1 (Homo sapiens) | ||||||||
| Activity: | Heme oxygenase, with EC number 1.14.99.3 | ||||||||
| Related: | 1qq8, 1n3u | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME
Heme oxygenase catalyzes the first step in the oxidative degradation of heme. The crystal structure of heme oxygenase-1 (HO-1) reported here reveals a novel helical fold with the heme sandwiched between two helices. The proximal helix provides a heme iron ligand, His 25. Conserved glycines in the distal helix near the oxygen binding site allow close contact between the helix backbone and heme in addition to providing flexibility for substrate binding and product release. Regioselective oxygenation of the alpha-meso heme carbon is due primarily to steric influence of the distal helix.
Crystal structure of human heme oxygenase-1., Schuller DJ, Wilks A, Ortiz de Montellano PR, Poulos TL, Nat Struct Biol. 1999 Sep;6(9):860-7. PMID:10467099
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1n45 is a 2 chain structure of Heme oxygenase with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1qq8. Full crystallographic information is available from OCA.
See Also
Reference
- Schuller DJ, Wilks A, Ortiz de Montellano PR, Poulos TL. Crystal structure of human heme oxygenase-1. Nat Struct Biol. 1999 Sep;6(9):860-7. PMID:10467099 doi:10.1038/12319
