MolNFT v1 · #187766 · protein
NADPH-dependent cytochrome P450 reductase 2B from sorghum bicolor (SBCPR2B) -oxidized form of NADP+ complex
7SV0 · NADPH--cytochrome P450 reductase: “NADPH-dependent cytochrome P450 reductase 2B from sorghum bicolor (SBCPR2B) -oxidized form of NADP+ complex”. X-ray diffraction, 2 ligands (NAP, FAD), 2 pockets (best druggability 0.65). MolNFT v1…
- PDB
- 7SV0
- Type
- protein
- Length
- 389 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
- C5YJG8
- Ligands
- NAP, FAD
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 389 | 39% helix, 20% strand | C5YJG8 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 516 | 0.65 | 0.77 | 59 | NAP, FAD |
| 2 | 51 | 0.37 | 0.81 | 16 | empty |
Modifications
Observed in the structure: 1 cofactor, 1 covalent (flavinylation, covalent ligand).
Compared structures
- 7SV0 · NADPH-dependent cytochrome P450 reductase 2b from Sorghum bicolor (SbCPR2b) -oxidized… · the same entry in another collection · chain A against A, TM-score 1.00
- C5YJG8 · AlphaFold monomer V2.0 prediction for NADPH--cytochrome P450 reductase (C5YJG8) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 C5YJG8
- Elsewhere: RCSB PDB 7SV0 · PDBe 7SV0 · UniProt C5YJG8
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