Research workbench
ATPRR1 with NADP+ and (-)lariciresinol
Analyse ATPRR1 with NADP+ and (-)lariciresinol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CSE
- Type
- protein
- Length
- 1,853 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9FVQ6
- Ligands
- GFR, NDP
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F, A, B, D | — | protein | 309 | — | Q9FVQ6 |
| C | — | protein | 308 | — | Q9FVQ6 |
Ligands and binding sites
- GFR · 4-[[(3S,4S,5R)-4-(hydroxymethyl)-5-(3-methoxy-4-oxidanyl-phenyl)oxolan-3-yl]methyl]-2-methoxy-phenol · ligand · 6 copies · chains E, F, A, B, C, D
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 6 copies · chains E, F, A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- Q9FVQ6 · AlphaFold monomer V2.0 prediction for pinoresinol reductase 1 (Q9FVQ6) · a predicted model of the same protein · chain E 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 Q9FVQ6
- Elsewhere: RCSB PDB 7CSE · PDBe 7CSE · UniProt Q9FVQ6
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