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Crystal structure of leishmania braziliensis glucokinase

Analyse Crystal structure of leishmania braziliensis glucokinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EDI
Type
protein
Length
788 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucokinase
EC
2.7.1.2
UniProt
A4HPA0
Pockets
8 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGlucokinase (EC 2.7.1.2)protein39443% helix, 23% strandA4HPA0

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111880.830.84151empty
21940.650.8529empty
31590.640.8628empty
43980.590.7644empty
5500.360.8017empty

Interfaces

1 interface between chains.

  • A–B · 2378 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 6EDI · Crystal structure of Leishmania braziliensis glucokinase · the same entry in another collection · chain A against A, TM-score 1.00

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