MolNFT v1 · #21388 · protein
Crystal structure of human heme oxygenase in a complex with biliverdine
1S8C · Heme oxygenase 1: “Crystal structure of human heme oxygenase in a complex with biliverdine”. X-ray diffraction, 1 ligand (BLA), 7 pockets (best druggability 0.75). MolNFT v1 #21388 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1S8C
- Type
- protein
- Length
- 855 residues
- Chains
- 4
- 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
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Heme oxygenase 1 (EC 1.14.99.3) | protein | 214 | 77% helix, 0% strand | P09601 |
| D | Heme oxygenase 1 (EC 1.14.99.3) | protein | 213 | 69% helix, 0% strand | P09601 |
Ligands and binding sites
- BLA · Biliverdine IX alpha · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 409 | 0.75 | 0.85 | 41 | empty |
| 2 | 456 | 0.75 | 0.84 | 44 | empty |
| 3 | 439 | 0.75 | 0.84 | 41 | BLA |
| 4 | 338 | 0.73 | 0.85 | 41 | empty |
| 5 | 315 | 0.63 | 0.80 | 38 | empty |
Interfaces
2 interfaces between chains.
- C–D · 1175 Ų buried · 32 hydrogen bonds · protein-protein
- A–B · 71 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 P09601
- Elsewhere: RCSB PDB 1S8C · PDBe 1S8C · UniProt P09601
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