MolNFT v1 · #50303 · protein

Crystal structures of C2ALPHA-PI3 kinase px-domain domain indicate conformational change associated with ligand binding.

2RED · Phosphatidylinositol-4-phosphate 3-kinase C2 domain…: “Crystal structures of C2ALPHA-PI3 kinase px-domain domain indicate conformational change associated with…”. X-ray diffraction, 1 pocket (best druggability 0.36). MolNFT v1…

PDB: 2RED
Type: protein
Length: 114 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol-4-phosphate 3-kinase C2 domain- containing alpha polypeptide
EC: 2.7.1.154
UniProt: O00443
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol-4-phosphate 3-kinase C2 domain- containing alpha polypeptide (EC 2.7.1.154)	protein	114	39% helix, 21% strand	O00443

Ligands and binding sites

GOL · Glycerol · additive · 6 copies · 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	68	0.36	0.77	15	empty

Compared structures

2RED · Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change… · the same entry in another collection · chain A against A, TM-score 1.00
O00443 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4-phosphate 3-kinase C2… · a predicted model of the same protein · chain A against A, TM-score 0.87

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 O00443
Elsewhere: RCSB PDB 2RED · PDBe 2RED · UniProt O00443

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