Research workbench

Putative sugar kinases from Arabidopsis thaliana in complex with ADP

Analyse Putative sugar kinases from Arabidopsis thaliana in complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HTX
Type: protein
Length: 424 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.492
Source: Arabidopsis thaliana
Molecule: Putative xylulose kinase
UniProt: Q8L794
Ligands: ADP
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · resolution 1.492 · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative xylulose kinase	protein	424	36% helix, 23% strand	Q8L794

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A

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	431	0.60	0.76	64	empty
2	130	0.50	0.80	21	empty
3	117	0.47	0.79	26	ADP

Compared structures

5HTX · Putative sugar kinases from arabidopsis thaliana in complex with ADP · the same entry in another collection · chain A against A, TM-score 1.00
Q8L794 · AlphaFold monomer V2.0 prediction for D-ribulose kinase (Q8L794) · a predicted model of the same protein · 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 Q8L794
Elsewhere: RCSB PDB 5HTX · PDBe 5HTX · UniProt Q8L794

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.