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Structure of the RNA binding domain (residues 404-479) of the bacillus subtilis yxin protein
Analyse Structure of the RNA binding domain (residues 404-479) of the bacillus subtilis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G0C
- Type
- protein
- Length
- 68 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent RNA helicase dbpa
- EC
- 3.6.1.-
- UniProt
- P42305
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase dbpa (EC 3.6.1.-) | protein | 68 | 28% helix, 26% strand | P42305 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2G0C · Structure of the RNA binding domain (residues 404-479) of the Bacillus subtilis YxiN… · the same entry in another collection · chain A against A, TM-score 1.00
- P42305 · AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase dbpa (P42305) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P42305
- Elsewhere: RCSB PDB 2G0C · PDBe 2G0C · UniProt P42305
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