Research workbench
Structure of yeast POLY(A) polymerase with ATP and OLIGO(A)
Analyse Structure of yeast POLY(A) polymerase with ATP and OLIGO(A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q66
- Type
- protein + RNA
- Length
- 524 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-R(P*AP*AP*AP*AP*A)-3'; POLY(A) polymerase
- EC
- 2.7.7.19
- UniProt
- P29468
- Ligands
- ATP, MG
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | 5'-R(P*AP*AP*AP*AP*A)-3' | rna | 5 | — | — |
| A | POLY(A) polymerase (EC 2.7.7.19) | protein | 519 | 45% helix, 17% strand | P29468 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains X, A
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 17 copies · chains X, A
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 | 914 | 0.81 | 0.83 | 91 | MG, ATP, EDO |
| 2 | 144 | 0.46 | 0.77 | 22 | EDO |
| 3 | 68 | 0.34 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- X–A · 914 Ų buried · 14 hydrogen bonds · protein-nucleic
Compared structures
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 P29468
- Elsewhere: RCSB PDB 2Q66 · PDBe 2Q66 · UniProt P29468
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