Structure of PDB 4rhu Chain E Binding Site BS01

Receptor Information
>4rhu Chain E (length=169) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ELYPGDIKSVLLTAEQIQARIAELGEQIGNDYRTGQDLLLITVLKGAVLF
VTDLARAIPVPTQFEFMAVSSILKDLDRDIHGRDVLIVEDVVDSGLTLSW
LSRNLTSRNPRSLRVCTLLRKPDAVHANVEIAYVGFDIPNDFVVGYGLDY
DERYRDLSYIGTLDPRVYQ
Ligand information
Ligand ID45T
InChIInChI=1S/C12H21N5O9P2/c13-12-15-10-9(11(18)16-12)14-7-17(10)5-8(26-2-4-28(22,23)24)6-25-1-3-27(19,20)21/h7-8H,1-6H2,(H2,19,20,21)(H2,22,23,24)(H3,13,15,16,18)/t8-/m0/s1
InChIKeyKFMQQVHVLQIQPE-QMMMGPOBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1nc2c(n1CC(COCCP(=O)(O)O)OCCP(=O)(O)O)N=C(NC2=O)N
ACDLabs 12.01O=P(O)(O)CCOCC(Cn2c1N=C(N)NC(c1nc2)=O)OCCP(O)(O)=O
OpenEye OEToolkits 1.7.6c1nc2c(n1C[C@@H](COCCP(=O)(O)O)OCCP(=O)(O)O)N=C(NC2=O)N
CACTVS 3.385NC1=Nc2n(C[CH](COCC[P](O)(O)=O)OCC[P](O)(O)=O)cnc2C(=O)N1
CACTVS 3.385NC1=Nc2n(C[C@@H](COCC[P](O)(O)=O)OCC[P](O)(O)=O)cnc2C(=O)N1
FormulaC12 H21 N5 O9 P2
Name{[(2S)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)propane-1,2-diyl]bis(oxyethane-2,1-diyl)}bis(phosphonic acid)
ChEMBL
DrugBank
ZINCZINC000095582835
PDB chain4rhu Chain E Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4rhu First Crystal Structures of Mycobacterium tuberculosis 6-Oxopurine Phosphoribosyltransferase: Complexes with GMP and Pyrophosphate and with Acyclic Nucleoside Phosphonates Whose Prodrugs Have Antituberculosis Activity.
Resolution2.573 Å
Binding residue
(original residue number in PDB)		V124 D126 S127 G128 T130 K154 F175 V176 D182
Binding residue
(residue number reindexed from 1)		V91 D93 S94 G95 T97 K121 F142 V143 D149
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E122 D123 D126 F175 R188
Catalytic site (residue number reindexed from 1) E89 D90 D93 F142 R155
Enzyme Commision number 2.4.2.8: hypoxanthine phosphoribosyltransferase.
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4rhu, PDBe:4rhu, PDBj:4rhu
PDBsum4rhu
PubMed25915781
UniProtP9WHQ9|HGPRT_MYCTU Hypoxanthine-guanine phosphoribosyltransferase (Gene Name=hpt)

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