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Structure of the C-terminal domain of the polymerase cofactor of rabies virus: insights in function and evolution.
Analyse Structure of the C-terminal domain of the polymerase cofactor of rabies virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VYI
- Type
- protein
- Length
- 111 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase alpha subunit
- EC
- 2.7.7.48
- UniProt
- P22363
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase alpha subunit (EC 2.7.7.48) | protein | 111 | 60% helix, 9% strand | P22363 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1VYI · Structure of the c-terminal domain of the polymerase cofactor of rabies virus: insights… · 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 P22363
- Elsewhere: RCSB PDB 1VYI · PDBe 1VYI · UniProt P22363
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