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Arabidopsis thaliana rhizobiales-like phosphatase 2 complexed with tungstate

Analyse Arabidopsis thaliana rhizobiales-like phosphatase 2 complexed with tungstate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VJW
Type: protein
Length: 298 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rhizobiales-like phosphatase 2
EC: 3.1.3.48
UniProt: Q9SR62
Ligands: ZN, WO4
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rhizobiales-like phosphatase 2 (EC 3.1.3.48)	protein	298	35% helix, 18% strand	Q9SR62

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
WO4 · Tungstate(vi)ion · ion · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	98	0.38	0.76	24	ZN, WO4

Compared structures

5VJW · Arabidopsis thaliana Rhizobiales-like phosphatase 2 complexed with tungstate · the same entry in another collection · chain A against A, TM-score 1.00
Q9SR62 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase RLPH2 (Q9SR62) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9SR62
Elsewhere: RCSB PDB 5VJW · PDBe 5VJW · UniProt Q9SR62

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