MolNFT v1 · #98086 · protein
Structure of a product bound plant phosphatase
4KYQ · Phosphoglucan phosphatase LSF2, chloroplastic: “Structure of a product bound plant phosphatase”. X-ray diffraction, 2 pockets (best druggability 0.55). MolNFT v1 #98086 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4KYQ
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucan phosphatase LSF2, chloroplastic
- EC
- 3.1.3.-
- UniProt
- Q9SRK5
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucan phosphatase LSF2, chloroplastic (EC 3.1.3.-) | protein | 206 | 50% helix, 12% strand | Q9SRK5 |
Ligands and binding sites
- FLC · Citrate anion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.55 | 0.81 | 23 | FLC |
| 2 | 67 | 0.31 | 0.75 | 14 | empty |
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 Q9SRK5
- Elsewhere: RCSB PDB 4KYQ · PDBe 4KYQ · UniProt Q9SRK5
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