Research workbench
Oryza sativa phytoene desaturase inhibited by norflurazon
Analyse Oryza sativa phytoene desaturase inhibited by norflurazon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MOG
- Type
- protein
- Length
- 2,345 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A2XDA1
- Ligands
- FAD, NRF
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 467 | — | A2XDA1 |
| B | — | protein | 472 | — | A2XDA1 |
| C, D | — | protein | 470 | — | A2XDA1 |
| E | — | protein | 466 | — | A2XDA1 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 5 copies · chains A, B, C, D, E
- NRF · Norflurazon · ligand · 5 copies · chains A, B, C, D, E
- IMD · Imidazole · additive · 6 copies · chains A, B, D
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 5 copies · chains A, D, B, E
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 A2XDA1
- Elsewhere: RCSB PDB 5MOG · PDBe 5MOG · UniProt A2XDA1
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