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Crystal structure of human phosphoserine phosphatase
Analyse Crystal structure of 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
- 1NNL
- Type
- protein
- Length
- 412 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-3-phosphoserine phosphatase
- EC
- 3.1.3.3
- UniProt
- P78330
- Ligands
- CA, CL
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-3-phosphoserine phosphatase (EC 3.1.3.3) | protein | 205 | 44% helix, 20% strand | P78330 |
| B | L-3-phosphoserine phosphatase (EC 3.1.3.3) | protein | 207 | 42% helix, 19% strand | P78330 |
Ligands and binding sites
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 | 242 | 0.58 | 0.79 | 29 | CL, CA |
| 2 | 203 | 0.55 | 0.79 | 29 | CL, CA |
| 3 | 72 | 0.36 | 0.76 | 9 | empty |
Interfaces
1 interface between chains.
- A–B · 11 Ų buried · 0 hydrogen bonds · protein-protein
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 1NNL · PDBe 1NNL · UniProt P78330
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