Research workbench
Ferredoxin-NADP(H) reductase mutant with ala 266 replaced by tyr (A266Y) and residues 267-272 deleted.
Analyse Ferredoxin-NADP(H) reductase mutant with ala 266 replaced by tyr (A266Y) and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K1X
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9L6V3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 251 | — | Q9L6V3 |
Compared structures
- 4K1X · Ferredoxin-NADP(H) Reductase mutant with Ala 266 replaced by Tyr (A266Y) and residues… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9L6V3 · AlphaFold monomer V2.0 prediction for FLAVODOXIN/FERREDOXIN--NADP reductase (Q9L6V3) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9L6V3
- Elsewhere: RCSB PDB 4K1X · PDBe 4K1X · UniProt Q9L6V3
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