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Crystal structure of apo heme oxygenase-1
Analyse Crystal structure of apo heme oxygenase-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IRM
- Type
- protein
- Length
- 580 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apo heme oxygenase-1
- EC
- 1.14.99.3
- UniProt
- P06762
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 59% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Apo heme oxygenase-1 (EC 1.14.99.3) | protein | 196 | 62% helix, 0% strand | P06762 |
| A | Apo heme oxygenase-1 (EC 1.14.99.3) | protein | 192 | 65% helix, 0% strand | P06762 |
| B | Apo heme oxygenase-1 (EC 1.14.99.3) | protein | 192 | 49% helix, 0% strand | P06762 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 795 | 0.70 | 0.76 | 85 | empty |
| 2 | 254 | 0.59 | 0.79 | 34 | empty |
| 3 | 73 | 0.57 | 0.87 | 21 | empty |
| 4 | 156 | 0.44 | 0.75 | 28 | empty |
| 5 | 110 | 0.42 | 0.76 | 11 | empty |
Interfaces
2 interfaces between chains.
- A–B · 321 Ų buried · 4 hydrogen bonds · protein-protein
- C–A · 305 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P06762
- Elsewhere: RCSB PDB 1IRM · PDBe 1IRM · UniProt P06762
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