Research workbench
Crystal structure of human heme oxygenase 1 H25R with biliverdin bound
Analyse Crystal structure of human heme oxygenase 1 H25R with biliverdin bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BTQ
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme oxygenase 1
- EC
- 1.14.99.3
- UniProt
- P09601
- Ligands
- BLA, SO4
- Pockets
- 5 · 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 1 (EC 1.14.99.3) | protein | 213 | 77% helix, 0% strand | P09601 |
| B | Heme oxygenase 1 (EC 1.14.99.3) | protein | 215 | 76% helix, 0% strand | P09601 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 391 | 0.76 | 0.85 | 40 | BLA |
| 2 | 402 | 0.75 | 0.85 | 41 | BLA |
| 3 | 306 | 0.62 | 0.79 | 36 | empty |
| 4 | 160 | 0.45 | 0.76 | 21 | empty |
| 5 | 104 | 0.44 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1193 Ų buried · 24 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 P09601
- Elsewhere: RCSB PDB 5BTQ · PDBe 5BTQ · UniProt P09601
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