Research workbench
K20A RNA dependent RNA polymerase mutant from foot-and-mouth disease virus complexed with an RNA
Analyse K20A RNA dependent RNA polymerase mutant from foot-and-mouth disease virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4X2B
- Type
- protein + RNA
- Length
- 490 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA dependent RNA polymerase; RNA template; RNA primer
- EC
- 2.7.7.48
- UniProt
- P03311
- Ligands
- MG
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA dependent RNA polymerase (EC 2.7.7.48) | protein | 477 | 43% helix, 17% strand | P03311 |
| B | RNA template | rna | 7 | — | — |
| C | RNA primer | rna | 6 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1190 | 0.78 | 0.81 | 88 | MG |
| 2 | 200 | 0.72 | 0.88 | 31 | empty |
| 3 | 60 | 0.29 | 0.74 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1023 Ų buried · 22 hydrogen bonds · protein-nucleic
- A–C · 682 Ų buried · 10 hydrogen bonds · protein-nucleic
- B–C · 246 Ų buried · 21 hydrogen bonds · nucleic-nucleic
Compared structures
- 4X2B · K20A RNA dependent RNA polymerase mutant from Foot-and-Mouth disease Virus complexed with… · 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 P03311
- Elsewhere: RCSB PDB 4X2B · PDBe 4X2B · UniProt P03311
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