Structure of PDB 2bgu Chain A Binding Site BS01

Receptor Information
>2bgu Chain A (length=328) Species: 10665 (Tequatrovirus T4) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSNLAILSAQKFMAKYKSKIYYLFTDIRLPFSQSE
EELLIKSPIKVISQGINLDIAKAAHKKVDNVIEFEYFPIEQYKIHMNDFQ
LSKPTKKTLDVIYGGSFRSGQRESKMVEFLFDTGLNIEFFGNAREKQFKN
PKYPWTKAPVFTGKIPMNMVSEKNSQAIAALIIGDKNYNDNFITLRVWET
MASDAVMLIDEEFDTKHRIINDARFYVNNRAELIDRVNELKHSDVLRKEM
LSIQHDILNKTRAKKAEWQDAFKKAIDL
Ligand information
Ligand IDUDP
InChIInChI=1S/C9H14N2O12P2/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(22-8)3-21-25(19,20)23-24(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
InChIKeyXCCTYIAWTASOJW-XVFCMESISA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)OP(=O)(O)O)O)O
CACTVS 3.370O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
CACTVS 3.370O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)O)O)O
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O
FormulaC9 H14 N2 O12 P2
NameURIDINE-5'-DIPHOSPHATE
ChEMBLCHEMBL130266
DrugBankDB03435
ZINCZINC000004490939
PDB chain2bgu Chain A Residue 353 [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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PDB2bgu Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		G188 S189 R195 F213 K237 I238 M240 R269 E272
Binding residue
(residue number reindexed from 1)		G165 S166 R172 F190 K214 I215 M217 R246 E249
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E22 D100 R191
Catalytic site (residue number reindexed from 1) E22 D91 R168
Enzyme Commision number 2.4.1.27: DNA beta-glucosyltransferase.
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
GO:0033821 DNA beta-glucosyltransferase activity
Biological Process
GO:0006304 DNA modification
GO:0019049 virus-mediated perturbation of host defense response
GO:0052170 symbiont-mediated suppression of host innate immune response
GO:0099018 symbiont-mediated evasion of host restriction-modification system

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2bgu, PDBe:2bgu, PDBj:2bgu
PDBsum2bgu
PubMed8062817
UniProtP04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)

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