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Crystal structure of the rat cytosolic PCK1, acetylated on LYS244

Analyse Crystal structure of the rat cytosolic PCK1, acetylated on LYS244 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6YI9
Type: protein
Length: 620 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
EC: 4.1.1.32
UniProt: P07379
Pockets: 8 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (EC 4.1.1.32)	protein	620	30% helix, 24% strand	P07379

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 20 copies · chains A

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

Pockets

8 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	750	0.78	0.82	71	EDO
2	55	0.72	0.99	17	EDO
3	221	0.61	0.81	29	EDO
4	89	0.47	0.81	16	empty
5	107	0.46	0.79	25	empty

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

6YI9 · Crystal structure of the rat cytosolic PCK1, acetylated on Lys244 · the same entry in another collection · chain A against A, TM-score 1.00

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 P07379
Elsewhere: RCSB PDB 6YI9 · PDBe 6YI9 · UniProt P07379

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