Research workbench
Crystal structure of human tRNA dihydrouridine synthase (20) dsrbd E423A mutant
Analyse Crystal structure of human tRNA dihydrouridine synthase (20) dsrbd E423A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F00
- Type
- protein
- Length
- 289 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9NX74
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 99 | — | Q9NX74 |
| A, C | — | protein | 95 | — | Q9NX74 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 10 copies · chains B, C, A
- GOL · Glycerol · additive · 5 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6F00 · Crystal Structure of human tRNA dihydrouridine synthase (20) dsRBD E423A mutant · the same entry in another collection · chain B against B, TM-score 1.00
- Q9NX74 · AlphaFold monomer V2.0 prediction for tRNA-DIHYDROURIDINE(20) synthase [NAD(P)+]-like… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q9NX74
- Elsewhere: RCSB PDB 6F00 · PDBe 6F00 · UniProt Q9NX74
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