Structure of PDB 1y6g Chain A Binding Site BS01
Receptor Information
>1y6g Chain A (length=392) Species:
10665
(Tequatrovirus T4) [
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MGSMRICIFMARGLEGCGVTKFSLEQRDWFIKNGHEVTLVYAKDKSFTRT
SSHDHKSFSIPVILAKEYDKALKLVNDCDILIINSVPATSVQEATINNYK
KLLDNIKPSIRVVVYQHDHSVLSLRRNLGLEETVRRADVIFSHSDNGDFN
KVLMKEWYPAPTVYNFQPPMDIVKVRSTYWKDVSEINMNINRWIGRTTTW
KGFYQMFDFHEKFLKPAGKSTVMEGLERSPAFIAIKEKGIPYEYYGNREI
DKMNLAPNQPAQILDCYINSEMLERMSKSGFGYQLSKLNQKYLQRSLEYT
HLELGACGTIPVFWKSTGENLKFRVDNTPLTSHDSGIIWFDENDMESTFE
RIKELSSDRALYDREREKAYEFLYQHQDSSFCFKEQFDIITK
Ligand information
>1y6g Chain C (length=13) [
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gatactuagatag
Receptor-Ligand Complex Structure
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PDB
1y6g
Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
T1206 T1207 W1208 E1235 R1236 S1237 A1239
Binding residue
(residue number reindexed from 1)
T198 T199 W200 E227 R228 S229 A231
Enzymatic activity
Enzyme Commision number
2.4.1.26
: DNA alpha-glucosyltransferase.
Gene Ontology
Molecular Function
GO:0016757
glycosyltransferase activity
GO:0033820
DNA alpha-glucosyltransferase activity
Biological Process
GO:0006304
DNA modification
GO:0019049
virus-mediated perturbation of host defense response
GO:0039504
symbiont-mediated suppression of host adaptive immune response
GO:0098672
symbiont-mediated suppression of host CRISPR-cas system
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:1y6g
,
PDBe:1y6g
,
PDBj:1y6g
PDBsum
1y6g
PubMed
16081100
UniProt
P04519
|GSTA_BPT4 DNA alpha-glucosyltransferase (Gene Name=agt)
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