Research workbench
Psph human phosphoserine phosphatase
Analyse Psph human phosphoserine phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HYJ
- Type
- protein
- Length
- 444 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoserine phosphatase
- EC
- 3.1.3.3
- UniProt
- P78330
- Ligands
- SEP, SER, CA
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoserine phosphatase (EC 3.1.3.3) | protein | 221 | 47% helix, 19% strand | P78330 |
| B | Phosphoserine phosphatase (EC 3.1.3.3) | protein | 223 | 42% helix, 18% strand | P78330 |
Ligands and binding sites
- SEP · Phosphoserine · ligand · 2 copies · chains A, B
- SER · Serine · ligand · chains B
- CA · Calcium ion · metal · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.76 | 0.92 | 34 | SEP, CA |
| 2 | 247 | 0.60 | 0.80 | 30 | CA |
| 3 | 137 | 0.40 | 0.74 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 122 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 P78330
- Elsewhere: RCSB PDB 6HYJ · PDBe 6HYJ · UniProt P78330
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