Structure of PDB 4rhu Chain A

Receptor sequence

>4rhuA (length=180) Species: 83332 (Mycobacterium tuberculosis H37Rv)

QTAELYPGDIKSVLLTAEQIQARIAELGEQIGNDYRETTGQDLLLITVLK
GAVLFVTDLARAIPVPTQFEFMAVSSYSGVVRILKDLDRDIHGRDVLIVE
DVVDSGLTLSWLSRNLTSRNPRSLRVCTLLRKPDAVHANVEIAYVGFDIP
NDFVVGYGLDYDERYRDLSYIGTLDPRVYQ

3D structure

• PDB: 4rhu First Crystal Structures of Mycobacterium tuberculosis 6-Oxopurine Phosphoribosyltransferase: Complexes with GMP and Pyrophosphate and with Acyclic Nucleoside Phosphonates Whose Prodrugs Have Antituberculosis Activity.
• Chain: A
• Resolution: 2.573 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E122 D123 D126 F175 R188
• Catalytic site (residue number reindexed from 1): E100 D101 D104 F153 R166
• Enzyme Commision number: 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	3QE	A	S127 G128 T130 K154 F175 V176 D182	S105 G106 T108 K132 F153 V154 D160	PDBbind-CN: -logKd/Ki=6.16,Ki=0.69uM
BS02	MG	A	E122 D123	E100 D101

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0000287 magnesium ion binding
• 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:0006177 GMP biosynthetic process
• GO:0006178 guanine salvage
• GO:0006188 IMP biosynthetic process
• GO:0032263 GMP salvage
• GO:0032264 IMP salvage
• GO:0043101 purine-containing compound salvage
• GO:0046100 hypoxanthine metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:4rhu, PDBe:4rhu, PDBj:4rhu
• PDBsum: 4rhu
• PubMed: 25915781
• UniProt: P9WHQ9|HGPRT_MYCTU Hypoxanthine-guanine phosphoribosyltransferase (Gene Name=hpt)