Structure of PDB 4lrl Chain A Binding Site BS02

Receptor Information
>4lrl Chain A (length=451) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AMTIPYKEQRLPIEKVFRDPVHNYIHVQHQVILDLINSAEVQRLRRIKQL
GTSSFTFHGAEHSRFSHSLGVYEITRRICEIFQRNYSVERLGENGWNDDE
RLITLCAALLHDVGHGPYSHTFEHIFDTNHEAITVQIITSPETEVYQILN
RVSADFPEKVASVITKQYPNPQVVQMISSQIDADRMDYLLRDAYFTGTEY
GTFDLTRILRVIRPYKGGIAFAMNGMHAVEDYIVSRYQMYVQVYFHPVSR
GMEVILDHLLHRAKELFENPEFDYDLQASLLVPFFKGDFTLQEYLKLDDG
VLSTYFTQWMDVPDSILGDLAKRFLMRKPLKSATFTNEKESAATIAYLRE
LIEKVGFNPKYYTAINSSYDLPYDFYRPNKDRHRTQIELMQKDGSLVELA
TVSPLVAALAGQSQGDERFYFPKEMLDQDLFDETYREFSSYIHNGALVLK
K
Ligand information
Ligand IDDGT
InChIInChI=1S/C10H16N5O13P3/c11-10-13-8-7(9(17)14-10)12-3-15(8)6-1-4(16)5(26-6)2-25-30(21,22)28-31(23,24)27-29(18,19)20/h3-6,16H,1-2H2,(H,21,22)(H,23,24)(H2,18,19,20)(H3,11,13,14,17)/t4-,5+,6+/m0/s1
InChIKeyHAAZLUGHYHWQIW-KVQBGUIXSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc2c(n1C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)N=C(NC2=O)N
CACTVS 3.341NC1=Nc2n(cnc2C(=O)N1)[CH]3C[CH](O)[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)O3
CACTVS 3.341NC1=Nc2n(cnc2C(=O)N1)[C@H]3C[C@H](O)[C@@H](CO[P@](O)(=O)O[P@](O)(=O)O[P](O)(O)=O)O3
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)CC3O
OpenEye OEToolkits 1.5.0c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@@](=O)(O)OP(=O)(O)O)O)N=C(NC2=O)N
FormulaC10 H16 N5 O13 P3
Name2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL477486
DrugBankDB02181
ZINCZINC000008215755
PDB chain4lrl Chain B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4lrl Mechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis.
Resolution2.35 Å
Binding residue
(original residue number in PDB)		F54 T55 R326
Binding residue
(residue number reindexed from 1)		F55 T56 R327
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008832 dGTPase activity
GO:0046872 metal ion binding
Biological Process
GO:0006203 dGTP catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4lrl, PDBe:4lrl, PDBj:4lrl
PDBsum4lrl
PubMed24338016
UniProtQ836G9

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