Research workbench
Tetragonal structure of mutant V173I of 3D polymerase from foot-and- mouth disease virus
Analyse Tetragonal structure of mutant V173I of 3D polymerase from foot-and- mouth… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N95
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3D polymerase
- UniProt
- A4H1Z0
- Ligands
- 3PO
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3D polymerase | protein | 476 | 41% helix, 18% strand | A4H1Z0 |
Ligands and binding sites
- 3PO · Triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 985 | 0.70 | 0.74 | 90 | 3PO |
Compared structures
- 5N95 · Tetragonal structure of mutant V173I of 3D polymerase from Foot-and-Mouth Disease Virus · 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 A4H1Z0
- Elsewhere: RCSB PDB 5N95 · PDBe 5N95 · UniProt A4H1Z0
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