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Solution structure of the C-terminal domain of the vaccinia virus DNA polymerase processivity factor component A20 fused to a short peptide from the viral DNA polymerase E9.
Analyse Solution structure of the C-terminal domain of the vaccinia virus DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZXP
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase processivity factor component A20,DNA polymerase processivity factor…
- UniProt
- P20995
- Pockets
- 2 · best druggability 0.42
Structure
solution nmr · 1 distinct chain · 58% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase processivity factor component A20,DNA polymerase processivity factor component E9 | protein | 151 | 58% helix, 9% strand | P20995 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.42 | 0.77 | 16 | empty |
| 2 | 79 | 0.33 | 0.75 | 18 | empty |
Compared structures
- 6ZXP · Solution structure of the C-terminal domain of the vaccinia virus DNA polymerase… · 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 P20995
- Elsewhere: RCSB PDB 6ZXP · PDBe 6ZXP · UniProt P20995
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