Structure of PDB 1sxp Chain B Binding Site BS02
Receptor Information
>1sxp Chain B (length=351) Species:
10665
(Tequatrovirus T4) [
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MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTD
IRLPFSQSWPNVKNRPWAYLYTEEELLIKSPIKVISQGINLDIAKAAHKK
VDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMV
EFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQA
IAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV
NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAID
L
Ligand information
>1sxp Chain D (length=12) [
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ctatctgagtat
Receptor-Ligand Complex Structure
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PDB
1sxp
Structural evidence of a passive base flipping mechanism for {beta}-Glucosyltransferase
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
K16 R217 K219 Q220 G236 K237
Binding residue
(residue number reindexed from 1)
K16 R217 K219 Q220 G236 K237
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.
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
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Biological Process
External links
PDB
RCSB:1sxp
,
PDBe:1sxp
,
PDBj:1sxp
PDBsum
1sxp
PubMed
15178685
UniProt
P04547
|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)
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