MolNFT v1 · #12297 · protein

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

1KCM · Phosphatidylinositol transfer protein alpha: “Crystal structure of mouse pitp alpha void of bound phospholipid at 2.0 ångströms resolution”. X-ray diffraction, 1 pocket (best druggability 0.70). MolNFT v1 #12297 on GenesisL1: 3D…

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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