Structure of PDB 1c3j Chain A

Receptor sequence
>1c3jA (length=333) Species: 10665 (Tequatrovirus T4) [Search protein sequence]
MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSNLAILSAQKFMAKYKSKIYYLFTDIRLPFSQSA
YLYTEEELLIKSPIKVISQGINLDIAKAAHKKVDNVIEFEYFPIEQYKIH
MNDFQLSKPTKKTLDVIYGGSFRSGQRESKMVEFLFDTGLNIEFFGNARE
KQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQAIAALIIGDKNYNDNFITL
RVWETMASDAVMLIDEEFDTKHRIINDARFYVNNRAELIDRVNELKHSDV
LRKEMLSIQHDILNKTRAKKAEWQDAFKKAIDL
3D structure
PDB1c3j T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism.
ChainA
Resolution1.88 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 R173
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 R191 R195 F213 G214 K237 I238 M240 R269 E272 G170 R173 R177 F195 G196 K219 I220 M222 R251 E254
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:1c3j, PDBe:1c3j, PDBj:1c3j
PDBsum1c3j
PubMed10497034
UniProtP04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)

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