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Structure of the pleckstrin homology domain from phospholipase C delta in complex with inositol trisphosphate

Analyse Structure of the pleckstrin homology domain from phospholipase C delta in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MAI
Type: protein
Length: 119 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase C delta-1
EC: 3.1.4.11
UniProt: P10688
Ligands: I3P
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phospholipase C delta-1 (EC 3.1.4.11)	protein	119	29% helix, 31% strand	P10688

Ligands and binding sites

I3P · D-myo-inositol-1,4,5-triphosphate · 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	100	0.42	0.77	22	I3P

Compared structures

1MAI · Structure of the pleckstrin homology domain from phospholipase C delta in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P10688 · AlphaFold monomer V2.0 prediction for 1-phosphatidylinositol 4,5-bisphosphate… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P10688
Elsewhere: RCSB PDB 1MAI · PDBe 1MAI · UniProt P10688

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