Research workbench
Mutant K20E of RNA dependent RNA polymerase 3D from foot-and-mouth disease virus complexed with RNA
Analyse Mutant K20E of RNA dependent RNA polymerase 3D from foot-and-mouth disease… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WZQ
- Type
- protein + RNA
- Length
- 491 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA dependent-RNA polymerase 3D; RNA template; Rnaprimer
- UniProt
- A4H1Z0
- Ligands
- MN
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA dependent-RNA polymerase 3D | protein | 476 | 42% helix, 15% strand | A4H1Z0 |
| B | RNA template | rna | 8 | — | — |
| C | Rnaprimer | rna | 7 | — | — |
Ligands and binding sites
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 999 | 0.82 | 0.84 | 63 | empty |
| 2 | 136 | 0.60 | 0.85 | 21 | empty |
| 3 | 61 | 0.54 | 0.88 | 16 | empty |
| 4 | 63 | 0.52 | 0.86 | 15 | empty |
| 5 | 77 | 0.36 | 0.77 | 18 | MN |
Interfaces
3 interfaces between chains.
- A–B · 989 Ų buried · 24 hydrogen bonds · protein-nucleic
- A–C · 735 Ų buried · 12 hydrogen bonds · protein-nucleic
- B–C · 295 Ų buried · 33 hydrogen bonds · nucleic-nucleic
Compared structures
- 4WZQ · Mutant K20E of RNA dependent RNA polymerase 3D 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 4WZQ · PDBe 4WZQ · UniProt A4H1Z0
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