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Human adenosine kinase in complex with an acetylinic inhibitor

Analyse Human adenosine kinase in complex with an acetylinic inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2I6B
Type: protein
Length: 655 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenosine kinase
UniProt: Q5VXR3
Ligands: 89I
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenosine kinase	protein	329	36% helix, 22% strand	Q5VXR3
B	Adenosine kinase	protein	326	37% helix, 20% strand	Q5VXR3

Ligands and binding sites

89I · 5-[4-(dimethylamino)phenyl]-6-[(6-morpholin-4-ylpyridin-3-yl)ethynyl]pyrimidin-4-amine · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	870	0.75	0.79	85	89I
2	812	0.72	0.78	69	89I
3	59	0.28	0.73	16	empty

Compared structures

2I6B · Human Adenosine Kinase in Complex with An Acetylinic Inhibitor · 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 Q5VXR3
Elsewhere: RCSB PDB 2I6B · PDBe 2I6B · UniProt Q5VXR3

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