Research workbench
Steroid receptor RNA activator (sra) modification by the human pseudouridine synthase 1 (HPUS1P): RNA binding, activity, and atomic model
Analyse Steroid receptor RNA activator (sra) modification by the human pseudouridine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NZ7
- Type
- protein
- Length
- 303 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRNA pseudouridine synthase a, mitochondrial
- EC
- 5.4.99.12
- UniProt
- Q9Y606
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA pseudouridine synthase a, mitochondrial (EC 5.4.99.12) | protein | 303 | 35% helix, 23% strand | Q9Y606 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.54 | 0.78 | 24 | EPE |
| 2 | 85 | 0.39 | 0.77 | 19 | empty |
| 3 | 55 | 0.28 | 0.75 | 18 | empty |
Compared structures
- 4NZ7 · Steroid receptor RNA Activator (SRA) modification by the human Pseudouridine Synthase 1… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y606 · AlphaFold monomer V2.0 prediction for tRNA pseudouridine synthase a (Q9Y606) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9Y606
- Elsewhere: RCSB PDB 4NZ7 · PDBe 4NZ7 · UniProt Q9Y606
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