Research workbench
Structure of E. COLI rpph bound to RNA and three magnesium ions
Analyse Structure of E. COLI rpph bound to RNA and three magnesium ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4S2Y
- Type
- protein + RNA
- Length
- 157 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA pyrophosphohydrolase; RNA (5'-R(*(APC)*GP*U)-3')
- EC
- 3.6.1.-
- UniProt
- P0A776
- Ligands
- MG, CL, SO4
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA pyrophosphohydrolase (EC 3.6.1.-) | protein | 155 | 31% helix, 33% strand | P0A776 |
| B | RNA (5'-R(*(APC)*GP*U)-3') | rna | 2 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, B
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 436 Ų buried · 16 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
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 P0A776
- Elsewhere: RCSB PDB 4S2Y · PDBe 4S2Y · UniProt P0A776
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