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Phosphatidylinositol-specific phospholipase C in complex with myo-inositol

Analyse Phosphatidylinositol-specific phospholipase C in complex with myo-inositol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PTG
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol-specific phospholipase C
EC: 3.1.4.10
UniProt: P14262
Ligands: INS
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol-specific phospholipase C (EC 3.1.4.10)	protein	296	32% helix, 20% strand	P14262

Ligands and binding sites

INS · 1,2,3,4,5,6-hexahydroxy-cyclohexane · ligand · 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	140	0.45	0.77	24	INS

Compared structures

1PTG · Phosphatidylinositol-specific phospholipase C in complex with myo-inositol · the same entry in another collection · chain A against A, TM-score 1.00
P14262 · AlphaFold monomer V2.0 prediction for 1-phosphatidylinositol phosphodiesterase (P14262) · 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 P14262
Elsewhere: RCSB PDB 1PTG · PDBe 1PTG · UniProt P14262

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