Structure of PDB 2bgu Chain A

Receptor sequence
>2bguA (length=328) Species: 10665 (Tequatrovirus T4) [Search protein sequence]
MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSNLAILSAQKFMAKYKSKIYYLFTDIRLPFSQSE
EELLIKSPIKVISQGINLDIAKAAHKKVDNVIEFEYFPIEQYKIHMNDFQ
LSKPTKKTLDVIYGGSFRSGQRESKMVEFLFDTGLNIEFFGNAREKQFKN
PKYPWTKAPVFTGKIPMNMVSEKNSQAIAALIIGDKNYNDNFITLRVWET
MASDAVMLIDEEFDTKHRIINDARFYVNNRAELIDRVNELKHSDVLRKEM
LSIQHDILNKTRAKKAEWQDAFKKAIDL
3D structure
PDB2bgu Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 UDP A G188 S189 R195 F213 K237 I238 M240 R269 E272 G165 S166 R172 F190 K214 I215 M217 R246 E249
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

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Molecular Function
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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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