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Crystal structure of udp-glucose 4-epimerase GALE1 from mycobacterium tuberculosis

Analyse Crystal structure of udp-glucose 4-epimerase GALE1 from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LTT
Type
protein
Length
621 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Udp-glucose 4-epimerase
EC
5.1.3.2
UniProt
P9WN67
Ligands
NAD
Pockets
3 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUdp-glucose 4-epimerase (EC 5.1.3.2)protein31140% helix, 17% strandP9WN67
BUdp-glucose 4-epimerase (EC 5.1.3.2)protein31042% helix, 18% strandP9WN67

Ligands and binding sites

  • NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
  • ACT · Acetate ion · additive · 2 copies · 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15940.840.8968NAD, ACT
28100.820.8473NAD
33660.560.7436empty

Interfaces

1 interface between chains.

  • A–B · 1211 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • P9WN67 · AlphaFold monomer V2.0 prediction for udp-glucose 4-epimerase (P9WN67) · a predicted model of the same protein · chain B against A, TM-score 0.99

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