MolNFT v1 · #58786 · protein
The role of asn 242 in P450CIN
3BE0: “The role of asn 242 in P450CIN”. X-ray diffraction, 2 ligands (HEM, CNL), 11 pockets (best druggability 0.86). MolNFT v1 #58786 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3BE0
- Type
- protein
- Length
- 794 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P450CIN
- UniProt
- Q8VQF6
- Ligands
- HEM, CNL
- Pockets
- 11 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | P450CIN | protein | 397 | 42% helix, 11% strand | Q8VQF6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- CNL · 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 509 | 0.86 | 0.92 | 55 | HEM, CNL |
| 2 | 503 | 0.86 | 0.92 | 52 | HEM, CNL |
| 3 | 63 | 0.72 | 0.97 | 22 | empty |
| 4 | 562 | 0.66 | 0.76 | 53 | empty |
| 5 | 177 | 0.51 | 0.78 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1025 Ų buried · 18 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 Q8VQF6
- Elsewhere: RCSB PDB 3BE0 · PDBe 3BE0 · UniProt Q8VQF6
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