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Crystal structure of hypoxanthine-guanine phosphoribosyltransferase from thermoanaerobacter tengcongensis

Analyse Crystal structure of hypoxanthine-guanine phosphoribosyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1R3U
Type
protein
Length
357 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypoxanthine-guanine phosphoribosyltransferase
EC
2.4.2.8
UniProt
Q8R7L0
Ligands
MG
Pockets
4 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8)protein17926% helix, 32% strandQ8R7L0
BHypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8)protein17830% helix, 33% strandQ8R7L0

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • ACT · Acetate ion · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13230.580.7631MG, ACT
23170.560.7628MG
3580.330.779empty
4520.250.7212empty

Interfaces

1 interface between chains.

  • A–B · 840 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 1R3U · Crystal Structure of Hypoxanthine-Guanine Phosphoribosyltransferase from… · the same entry in another collection · chain A against A, TM-score 1.00

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