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Crystal structure of mouse pitp alpha void of bound phospholipid at 2.0 ångströms resolution

Analyse Crystal structure of mouse pitp alpha void of bound phospholipid at 2.0… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KCM
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol transfer protein alpha
UniProt: P53810
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol transfer protein alpha	protein	256	34% helix, 28% strand	P53810

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	812	0.70	0.76	63	empty

Compared structures

1KCM · Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms… · the same entry in another collection · chain A against A, TM-score 1.00
P53810 · AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein alpha isoform… · a predicted model of the same protein · chain A against A, TM-score 0.86

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 P53810
Elsewhere: RCSB PDB 1KCM · PDBe 1KCM · UniProt P53810

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