MolNFT v1 · #80531 · protein
The role of I87 of CYP158A2 in oxidative coupling reaction
3TZO · Putative cytochrome P450: “The role of I87 of CYP158A2 in oxidative coupling reaction”. X-ray diffraction, 2 ligands (HEM, SPM), 3 pockets (best druggability 0.80). MolNFT v1 #80531 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3TZO
- Type
- protein
- Length
- 804 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cytochrome P450
- UniProt
- Q9FCA6
- Ligands
- HEM, SPM
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative cytochrome P450 | protein | 402 | 50% helix, 10% strand | Q9FCA6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- SPM · Spermine · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.80 | 0.82 | 87 | HEM |
| 2 | 1172 | 0.80 | 0.81 | 98 | HEM |
| 3 | 1094 | 0.76 | 0.79 | 106 | empty |
Interfaces
1 interface between chains.
- A–B · 379 Ų buried · 3 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 Q9FCA6
- Elsewhere: RCSB PDB 3TZO · PDBe 3TZO · UniProt Q9FCA6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.