Research workbench
Crystal structure of bacterial serine phosphatase bearing R161E mutation
Analyse Crystal structure of bacterial serine phosphatase bearing R161E mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IHV
- Type
- protein
- Length
- 221 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Staphylococcus aureus
- Molecule
- Phosphorylated protein phosphatase
- EC
- 3.1.3.16
- UniProt
- Q9RL81
- Ligands
- MG
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphorylated protein phosphatase (EC 3.1.3.16) | protein | 221 | 30% helix, 29% strand | Q9RL81 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6IHV · Crystal structure of bacterial serine phosphatase bearing R161E mutation · 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 Q9RL81
- Elsewhere: RCSB PDB 6IHV · PDBe 6IHV · UniProt Q9RL81
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