Structure of PDB 1jg6 Chain A

Receptor sequence
>1jg6A (length=351) Species: 10665 (Tequatrovirus T4) [Search protein sequence]
MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTD
IRLPFSQSWPNVKNRPWAYLYTEEELLIKSPIKVISQGINLDIAKAAHKK
VDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMV
EFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQA
IAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV
NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAID
L
3D structure
PDB1jg6 High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding.
ChainA
Resolution1.9 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 F72 D100 R191
Catalytic site (residue number reindexed from 1) E22 F72 D100 R191
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 V18 G188 S189 R191 R195 F213 G214 K237 I238 M240 V243 R269 E272 V18 G188 S189 R191 R195 F213 G214 K237 I238 M240 V243 R269 E272
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:1jg6, PDBe:1jg6, PDBj:1jg6
PDBsum1jg6
PubMed11493010
UniProtP04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)

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