Research workbench

Rat pitp-beta complexed to phosphatidylcholine

Analyse Rat pitp-beta complexed to phosphatidylcholine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2A1L
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol transfer protein beta isoform
UniProt: P53812
Ligands: PCW
Pockets: 2 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol transfer protein beta isoform	protein	269	34% helix, 27% strand	P53812

Ligands and binding sites

PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	803	0.88	0.90	75	PCW
2	65	0.35	0.77	12	empty

Compared structures

2A1L · Rat PITP-Beta Complexed to Phosphatidylcholine · the same entry in another collection · chain A against A, TM-score 1.00
P53812 · AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein beta isoform… · 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 P53812
Elsewhere: RCSB PDB 2A1L · PDBe 2A1L · UniProt P53812

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