Research workbench
A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductases.
Analyse A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BF4
- Type
- protein
- Length
- 1,290 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16603
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 645 | — | P16603 |
Compared structures
- 2BF4 · A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel… · the same entry in another collection · chain A against A, TM-score 1.00
- 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 1.00
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
- Elsewhere: RCSB PDB 2BF4 · PDBe 2BF4 · UniProt P16603
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