Research workbench
Mutant P44S M296I of foot-and-mouth disease virus RNA-dependent RNA polymerase
Analyse Mutant P44S M296I of foot-and-mouth disease virus RNA-dependent RNA polymerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NL0
- Type
- protein + RNA
- Length
- 488 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3D polymerase; 5'-R(P*UP*GP*GP*GP*CP*CP*C)-3'; 5'-R(*G*GP*GP*CP*CP*C)-3'
- UniProt
- Q9QCE4
- Ligands
- MG
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3D polymerase | protein | 475 | 42% helix, 19% strand | Q9QCE4 |
| B | 5'-R(P*UP*GP*GP*GP*CP*CP*C)-3' | rna | 7 | — | — |
| C | 5'-R(*G*GP*GP*CP*CP*C)-3' | rna | 6 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
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 | 1195 | 0.79 | 0.81 | 91 | MG |
| 2 | 146 | 0.66 | 0.88 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–B · 841 Ų buried · 24 hydrogen bonds · protein-nucleic
- A–C · 612 Ų buried · 6 hydrogen bonds · protein-nucleic
- B–C · 289 Ų buried · 25 hydrogen bonds · nucleic-nucleic
Compared structures
- 3NL0 · Mutant P44S M296I of Foot-and-mouth disease Virus RNA-dependent RNA 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 Q9QCE4
- Elsewhere: RCSB PDB 3NL0 · PDBe 3NL0 · UniProt Q9QCE4
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