Research workbench
NADPH-cytochrome P450 reductase in an open conformation
Analyse NADPH-cytochrome P450 reductase in an open conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ES9
- Type
- protein
- Length
- 1,553 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH--cytochrome P450 reductase
- EC
- 1.6.2.4
- UniProt
- P00388
- Ligands
- FAD, NAP, FMN
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 603 | 35% helix, 19% strand | P00388 |
| B | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 515 | 31% helix, 17% strand | P00388 |
| C | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 435 | 29% helix, 18% strand | P00388 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 3 copies · chains A, B, C
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- FMN · Flavin mononucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1129 | 0.76 | 0.78 | 71 | empty |
| 2 | 618 | 0.67 | 0.77 | 72 | FAD, NAP |
| 3 | 307 | 0.67 | 0.82 | 33 | empty |
| 4 | 315 | 0.66 | 0.81 | 36 | empty |
| 5 | 296 | 0.62 | 0.80 | 38 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1275 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 578 Ų buried · 4 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 P00388
- Elsewhere: RCSB PDB 3ES9 · PDBe 3ES9 · UniProt P00388
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