Research workbench
Wild type rat cypor bound with NADP+ - reduced form
Analyse Wild type rat cypor bound with NADP+ - reduced form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5URE
- Type
- protein
- Length
- 1,215 residues
- Chains
- 2
- 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
- FMN, FAD, NAP, PO4
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 608 | 37% helix, 21% strand | P00388 |
| B | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 607 | 36% helix, 22% strand | P00388 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 807 | 0.82 | 0.85 | 87 | empty |
| 2 | 470 | 0.78 | 0.86 | 56 | FMN, FAD |
| 3 | 834 | 0.78 | 0.81 | 72 | empty |
| 4 | 723 | 0.77 | 0.81 | 81 | FMN, FAD |
| 5 | 399 | 0.65 | 0.79 | 34 | NAP |
Interfaces
1 interface between chains.
- A–B · 731 Ų buried · 8 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 5URE · PDBe 5URE · UniProt P00388
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