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Crystal structure of catalytic domain of ptprq

Analyse Crystal structure of catalytic domain of ptprq in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IKC
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphotidylinositol phosphatase ptprq
EC: 3.1.3.48
UniProt: Q9UMZ3
Ligands: SO4, CL
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphotidylinositol phosphatase ptprq (EC 3.1.3.48)	protein	274	37% helix, 22% strand	Q9UMZ3

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
CL · Chloride 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.30	0.75	18	SO4

Compared structures

4IKC · Crystal Structure of catalytic domain of PTPRQ · the same entry in another collection · chain A against A, TM-score 1.00
Q9UMZ3 · AlphaFold monomer V2.0 prediction for phosphatidylinositol phosphatase ptprq (Q9UMZ3) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9UMZ3
Elsewhere: RCSB PDB 4IKC · PDBe 4IKC · UniProt Q9UMZ3

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