Research workbench
Divergent evolutions of trinucleotide polymerization revealed by an archaeal cca-adding enzyme structure
Analyse Divergent evolutions of trinucleotide polymerization revealed by an archaeal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UET
- Type
- protein
- Length
- 429 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRNA nucleotidyltransferase
- EC
- 2.7.7.25
- UniProt
- O28126
- Ligands
- CA, MG
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA nucleotidyltransferase (EC 2.7.7.25) | protein | 429 | 44% helix, 20% strand | O28126 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A
- MG · Magnesium ion · metal · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 491 | 0.64 | 0.76 | 42 | empty |
| 2 | 94 | 0.61 | 0.88 | 19 | empty |
| 3 | 321 | 0.51 | 0.73 | 27 | ACT, CA |
| 4 | 54 | 0.28 | 0.75 | 16 | empty |
Compared structures
- 1UET · Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding… · the same entry in another collection · chain A against A, TM-score 1.00
- O28126 · AlphaFold monomer V2.0 prediction for cca-adding enzyme (O28126) · 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 O28126
- Elsewhere: RCSB PDB 1UET · PDBe 1UET · UniProt O28126
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.