MolNFT v1 · #63766 · protein
Structure of chimeric yh cpr
3FJO · NADPH-cytochrome P450 reductase: “Structure of chimeric yh cpr”. X-ray diffraction, 2 ligands (FMN, FAD), 5 pockets (best druggability 0.54). MolNFT v1 #63766 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FJO
- Type
- protein
- Length
- 603 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH-cytochrome P450 reductase
- EC
- 1.6.2.4
- UniProt
- P16603, P16435
- Ligands
- FMN, FAD
- Pockets
- 5 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-cytochrome P450 reductase (EC 1.6.2.4) | protein | 603 | 38% helix, 21% strand | P16603, P16435 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.54 | 0.75 | 41 | FAD |
| 2 | 184 | 0.51 | 0.78 | 24 | empty |
| 3 | 92 | 0.45 | 0.80 | 22 | FMN |
| 4 | 92 | 0.32 | 0.73 | 16 | empty |
| 5 | 52 | 0.24 | 0.72 | 15 | empty |
Compared structures
- 3FJO · Structure of chimeric YH CPR · the same entry in another collection · chain A against A, TM-score 1.00
- P16435 · AlphaFold monomer V2.0 prediction for NADPH--cytochrome P450 reductase (P16435) · a predicted model of the same protein · chain A against A, TM-score 0.71
- P16603 · AlphaFold monomer V2.0 prediction for NADPH--cytochrome P450 reductase (P16603) · a predicted model of the same protein · chain A against A, TM-score 0.68
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 P16603
- Every structure of UniProt P16435
- Elsewhere: RCSB PDB 3FJO · PDBe 3FJO · UniProt P16603 · UniProt P16435
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