Research workbench
Hypothetical protein (probable phosphoserine phosph (PH0253) from pyrococcus horikoshii OT3
Analyse Hypothetical protein (probable phosphoserine phosph (PH0253) from pyrococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OM6
- Type
- protein
- Length
- 466 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable phosphoserine phosphatase
- EC
- 3.1.3.3
- UniProt
- O57991
- Ligands
- MG, SO4, CL
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable phosphoserine phosphatase (EC 3.1.3.3) | protein | 233 | 54% helix, 15% strand | O57991 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.73 | 0.96 | 24 | SO4 |
| 2 | 74 | 0.72 | 0.97 | 24 | SO4, MG |
| 3 | 449 | 0.69 | 0.80 | 55 | empty |
Interfaces
1 interface between chains.
- A–B · 1003 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 2OM6 · Hypothetical Protein (Probable Phosphoserine Phosph (PH0253) from Pyrococcus Horikoshii… · 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 O57991
- Elsewhere: RCSB PDB 2OM6 · PDBe 2OM6 · UniProt O57991
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