Research workbench
EMG1 N1-specific pseudouridine methyltransferase
Analyse EMG1 N1-specific pseudouridine methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FAI
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosomal RNA small subunit methyltransferase NEP1
- EC
- 2.1.1.-
- UniProt
- Q92979
- Ligands
- SAH, UNX
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosomal RNA small subunit methyltransferase NEP1 (EC 2.1.1.-) | protein | 209 | 29% helix, 26% strand | Q92979 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- UNX · Unknown atom or ion · ion · 12 copies · chains A
- CIT · Citric acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.57 | 0.81 | 23 | SAH, CIT |
Compared structures
- 5FAI · EMG1 N1-Specific Pseudouridine Methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
- Q92979 · AlphaFold monomer V2.0 prediction for ribosomal RNA small subunit methyltransferase NEP1… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q92979
- Elsewhere: RCSB PDB 5FAI · PDBe 5FAI · UniProt Q92979
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