Research workbench

Structure of a product bound plant phosphatase

Analyse Structure of a product bound plant phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KYR
Type: protein
Length: 208 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
Ligands: GLC, PO4
Pockets: 1 · best druggability 0.52

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	208	50% helix, 12% strand	Q9SRK5

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 22 copies · chains A
PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	189	0.52	0.78	24	GLC, PO4

Compared structures

4KYR · Structure of a product bound plant phosphatase · the same entry in another collection · chain A against A, TM-score 1.00
Q9SRK5 · AlphaFold monomer V2.0 prediction for phosphoglucan phosphatase LSF2, chloroplastic… · a predicted model of the same protein · chain A against A, TM-score 0.96

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 4KYR · PDBe 4KYR · UniProt Q9SRK5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.