Structure of PDB 1hgx Chain A

Receptor sequence

>1hgxA (length=164)

MDDLERVLYNQDDIQKRIRELAAELTEFYEDKNPVMICVLTGAVFFYTDL
LKHLDFQLEPDYIICSSLTISKDLKTNIEGRHVLVVEDIIDTGLTMYQLL
NNLQMRKPASLKVCTLCDKDIGKKAYDVPIDYCGFVVENRYIIGYGFDFH
NKYRNLPVIGILKE

3D structure

• PDB: 1hgx Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E102 D103 D106 Y156 R169
• Catalytic site (residue number reindexed from 1): E87 D88 D91 Y141 R154
• Enzyme Commision number: 2.4.2.22: xanthine phosphoribosyltransferase.
  2.4.2.8: hypoxanthine phosphoribosyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	5GP	A	D103 I104 D106 T107 G108 T110 K134 Y156 I157 F162	D88 I89 D91 T92 G93 T95 K119 Y141 I142 F147

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0000287 magnesium ion binding
• GO:0000310 xanthine phosphoribosyltransferase activity
• GO:0004422 hypoxanthine phosphoribosyltransferase activity
• GO:0016757 glycosyltransferase activity
• GO:0046872 metal ion binding
• GO:0052657 guanine phosphoribosyltransferase activity

Biological Process

• GO:0006166 purine ribonucleoside salvage
• GO:0006178 guanine salvage
• GO:0032263 GMP salvage
• GO:0032264 IMP salvage
• GO:0032265 XMP salvage
• GO:0046100 hypoxanthine metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1hgx, PDBe:1hgx, PDBj:1hgx
• PDBsum: 1hgx
• PubMed: 8679528
• UniProt: P51900|HGXR_TRIFO Hypoxanthine-guanine-xanthine phosphoribosyltransferase (Gene Name=HPT)