Research workbench
Crystal structure of the vaccinia polyadenylate polymerase heterodimer (apo form)
Analyse Crystal structure of the vaccinia polyadenylate polymerase heterodimer (apo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GAF
- Type
- protein
- Length
- 733 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase; POLY(A) polymerase catalytic…
- EC
- 2.1.1.57, 2.7.7.19
- UniProt
- P07617, P23371
- Pockets
- 10 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase (EC 2.1.1.57) | protein | 286 | 39% helix, 18% strand | P07617 |
| D | POLY(A) polymerase catalytic subunit (EC 2.7.7.19) | protein | 447 | 47% helix, 16% strand | P23371 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.74 | 0.81 | 61 | empty |
| 2 | 225 | 0.65 | 0.83 | 41 | empty |
| 3 | 309 | 0.59 | 0.78 | 39 | empty |
| 4 | 256 | 0.53 | 0.76 | 28 | empty |
| 5 | 209 | 0.49 | 0.75 | 29 | empty |
Interfaces
1 interface between chains.
- A–D · 1793 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2GAF · Crystal Structure of the Vaccinia Polyadenylate Polymerase Heterodimer (apo form) · 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 P07617
- Every structure of UniProt P23371
- Elsewhere: RCSB PDB 2GAF · PDBe 2GAF · UniProt P07617 · UniProt P23371
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