Research workbench
Mutagenesis and crystallographic studies of zymomonas mobilis tRNA- guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity
Analyse Mutagenesis and crystallographic studies of zymomonas mobilis tRNA- guanine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EFZ
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRNA-guanine transglycosylase
- EC
- 2.4.2.29
- UniProt
- P28720
- Ligands
- PRF, ZN
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA-guanine transglycosylase (EC 2.4.2.29) | protein | 372 | 45% helix, 18% strand | P28720 |
Ligands and binding sites
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 | 283 | 0.66 | 0.82 | 39 | PRF |
| 2 | 51 | 0.43 | 0.83 | 14 | empty |
| 3 | 50 | 0.34 | 0.79 | 11 | empty |
Compared structures
- 1EFZ · Mutagenesis and crystallographic studies of zymomonas mobilis tRNA-guanine… · the same entry in another collection · chain A against A, TM-score 1.00
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 P28720
- Elsewhere: RCSB PDB 1EFZ · PDBe 1EFZ · UniProt P28720
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