Research workbench
Crystal structure of human heme oxygenase-2 C127A (ho-2) with bound heme
Analyse Crystal structure of human heme oxygenase-2 C127A (ho-2) with bound heme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QPP
- Type
- protein
- Length
- 433 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme oxygenase 2
- EC
- 1.14.99.3
- UniProt
- P30519
- Ligands
- HEM
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heme oxygenase 2 (EC 1.14.99.3) | protein | 214 | 74% helix, 0% strand | P30519 |
| B | Heme oxygenase 2 (EC 1.14.99.3) | protein | 219 | 76% helix, 0% strand | P30519 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 434 | 0.77 | 0.85 | 42 | HEM |
| 2 | 429 | 0.74 | 0.84 | 46 | HEM |
| 3 | 379 | 0.63 | 0.78 | 33 | empty |
| 4 | 107 | 0.38 | 0.75 | 19 | empty |
| 5 | 61 | 0.33 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 675 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2QPP · Crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme · the same entry in another collection · chain A against A, TM-score 1.00
- P30519 · AlphaFold monomer V2.0 prediction for heme oxygenase 2 (P30519) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 2QPP · PDBe 2QPP · UniProt P30519
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