MolNFT v1 · #25130 · protein
Crystal structure of xenon bound rat heme-heme oxygenase-1 complex
1VGI · Heme oxygenase 1: “Crystal structure of xenon bound rat heme-heme oxygenase-1 complex”. X-ray diffraction, 2 ligands (HEM, XE), 1 pocket (best druggability 0.74). MolNFT v1 #25130 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1VGI
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme oxygenase 1
- EC
- 1.14.99.3
- UniProt
- P06762
- Ligands
- HEM, XE
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heme oxygenase 1 (EC 1.14.99.3) | protein | 212 | 75% helix, 0% strand | P06762 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- XE · Xenon · ion · chains A
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.74 | 0.86 | 36 | HEM, XE |
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 1VGI · PDBe 1VGI · UniProt P06762
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