MolNFT v1 · #23921 · protein
Divergent evolutions of trinucleotide polymerization revealed by an archaeal cca-adding enzyme structure
1UEV · TRNA nucleotidyltransferase: “Divergent evolutions of trinucleotide polymerization revealed by an archaeal cca-adding enzyme structure”. X-ray diffraction, 3 ligands (ATP, CA, MG), 2 pockets (best druggability 0.70). MolNFT v1…
- PDB
- 1UEV
- Type
- protein
- Length
- 431 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
- ATP, CA, MG
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA nucleotidyltransferase (EC 2.7.7.25) | protein | 431 | 43% helix, 21% strand | O28126 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 677 | 0.70 | 0.78 | 57 | MG, ATP |
| 2 | 329 | 0.51 | 0.73 | 29 | CA |
Compared structures
- 1UEV · 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 1UEV · PDBe 1UEV · UniProt O28126
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