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2.76 ångström crystal structure of a putative glucose-1-phosphate thymidylyltransferase from bacillus anthracis in complex with a sucrose.

Analyse 2.76 ångström crystal structure of a putative glucose-1-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3HL3
Type
protein
Length
246 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucose-1-phosphate thymidylyltransferase
EC
2.7.7.24
UniProt
Q81TP2
Ligands
GLC, FRU
Pockets
1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlucose-1-phosphate thymidylyltransferase (EC 2.7.7.24)protein24634% helix, 28% strandQ81TP2

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · chains A
  • FRU · beta-D-fructofuranose · sugar · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14510.680.7949GLC, FRU

Compared structures

  • 3HL3 · 2.76 Angstrom Crystal Structure of a Putative Glucose-1-Phosphate Thymidylyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00

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