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Crystal structure of human heme oxygenase-2
Analyse Crystal structure of human heme oxygenase-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UC8
- Type
- protein
- Length
- 839 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme oxygenase 2
- EC
- 1.14.14.18
- UniProt
- P30519
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heme oxygenase 2 (EC 1.14.14.18) | protein | 209 | 76% helix, 0% strand | P30519 |
| B, C, D | Heme oxygenase 2 (EC 1.14.14.18) | protein | 210 | 76% helix, 0% strand | P30519 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 483 | 0.76 | 0.84 | 43 | empty |
| 2 | 422 | 0.76 | 0.85 | 39 | empty |
| 3 | 456 | 0.75 | 0.84 | 42 | empty |
| 4 | 1163 | 0.75 | 0.77 | 97 | empty |
| 5 | 505 | 0.74 | 0.82 | 43 | empty |
Interfaces
5 interfaces between chains.
- A–D · 449 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 249 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 241 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 134 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 111 Ų buried · 1 hydrogen bond · 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 P30519
- Elsewhere: RCSB PDB 5UC8 · PDBe 5UC8 · UniProt P30519
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