Structure of PDB 1ixy Chain B Binding Site BS02
Receptor Information
>1ixy Chain B (length=351) Species:
10665
(Tequatrovirus T4) [
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MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTD
IRLPFSQSWPNVKNRPWAYLYTEEELLIKSPIKVISQGINLDIAKAAHKK
VDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMV
EFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQA
IAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV
NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAID
L
Ligand information
>1ixy Chain D (length=13) [
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gatactcagatag
Receptor-Ligand Complex Structure
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PDB
1ixy
A Base-flipping Mechanism for the T4 Phage beta-Glucosyltransferase and Identification of a Transition-state Analog
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
T17 S68 N70 F72 S192 N215
Binding residue
(residue number reindexed from 1)
T17 S68 N70 F72 S192 N215
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
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Molecular Function
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Biological Process
External links
PDB
RCSB:1ixy
,
PDBe:1ixy
,
PDBj:1ixy
PDBsum
1ixy
PubMed
12445783
UniProt
P04547
|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)
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