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Crystal structure of phosphoserine phosphatase in apo form
Analyse Crystal structure of phosphoserine phosphatase in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L7O
- Type
- protein
- Length
- 408 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoserine phosphatase
- EC
- 3.1.3.3
- UniProt
- Q58989
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoserine phosphatase (EC 3.1.3.3) | protein | 200 | 46% helix, 25% strand | Q58989 |
| B | Phosphoserine phosphatase (EC 3.1.3.3) | protein | 208 | 48% helix, 24% strand | Q58989 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.69 | 0.84 | 39 | empty |
| 2 | 173 | 0.63 | 0.84 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 451 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
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 Q58989
- Elsewhere: RCSB PDB 1L7O · PDBe 1L7O · UniProt Q58989
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