MolNFT v1 · #10393 · protein
Crystal structure of archaeosine tRNA-guanine transglycosylase from pyrococcus horikoshii
1IQ8: “Crystal structure of archaeosine tRNA-guanine transglycosylase from pyrococcus horikoshii”. X-ray diffraction, 2 ligands (ZN, MG), 13 pockets (best druggability 0.73). MolNFT v1 #10393 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1IQ8
- Type
- protein
- Length
- 1,154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Archaeosine tRNA-guanine transglycosylase
- EC
- 2.4.2.29
- UniProt
- O58843
- Ligands
- ZN, MG
- Pockets
- 13 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Archaeosine tRNA-guanine transglycosylase (EC 2.4.2.29) | protein | 577 | 42% helix, 21% strand | O58843 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 381 | 0.73 | 0.84 | 54 | empty |
| 2 | 60 | 0.70 | 0.98 | 28 | empty |
| 3 | 318 | 0.66 | 0.81 | 39 | empty |
| 4 | 217 | 0.60 | 0.81 | 28 | empty |
| 5 | 215 | 0.58 | 0.80 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 2216 Ų buried · 44 hydrogen bonds · protein-protein
Compared structures
- 1IQ8 · Crystal Structure of archaeosine tRNA-guanine transglycosylase from Pyrococcus horikoshii · the same entry in another collection · chain A against A, TM-score 1.00
- O58843 · AlphaFold monomer V2.0 prediction for tRNA-GUANINE(15) transglycosylase (O58843) · a predicted model of the same protein · chain A 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 O58843
- Elsewhere: RCSB PDB 1IQ8 · PDBe 1IQ8 · UniProt O58843
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