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Phosphatidylinositol transfer protein SEC14P from saccharomyces cerevisiae

Analyse Phosphatidylinositol transfer protein SEC14P from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AUA
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol transfer protein SEC14P
UniProt: P24280
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol transfer protein SEC14P	protein	296	50% helix, 9% strand	P24280

Ligands and binding sites

BOG · octyl beta-D-glucopyranoside · additive · 2 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	271	0.70	0.85	35	empty
2	439	0.67	0.79	54	BOG
3	131	0.59	0.85	21	empty

Compared structures

1AUA · Phosphatidylinositol transfer protein SEC14P from saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
P24280 · AlphaFold monomer V2.0 prediction for SEC14 cytosolic factor (P24280) · 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 P24280
Elsewhere: RCSB PDB 1AUA · PDBe 1AUA · UniProt P24280

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