Structure of PDB 1y6g Chain B

Receptor sequence
>1y6gB (length=393) Species: 10665 (Tequatrovirus T4) [Search protein sequence]
MGSMRICIFMARGLEGCGVTKFSLEQRDWFIKNGHEVTLVYAKDKSFTRT
SSHDHKSFSIPVILAKEYDKALKLVNDCDILIINSVPATSVQEATINNYK
KLLDNIKPSIRVVVYQHDHSVLSLRRNLGLEETVRRADVIFSHSDNGDFN
KVLMKEWYPEAPTVYNFQPPMDIVKVRSTYWKDVSEINMNINRWIGRTTT
WKGFYQMFDFHEKFLKPAGKSTVMEGLERSPAFIAIKEKGIPYEYYGNRE
IDKMNLAPNQPAQILDCYINSEMLERMSKSGFGYQLSKLNQKYLQRSLEY
THLELGACGTIPVFWKSTGENLKFRVDNTPLTSHDSGIIWFDENDMESTF
ERIKELSSDRALYDREREKAYEFLYQHQDSSFCFKEQFDIITK
3D structure
PDB1y6g Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase.
ChainB
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.26: DNA alpha-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 dna B L1119 S1120 R1123 P1238 L122 S123 R126 P231
BS02 dna B R1122 P1238 A1239 I1241 R125 P231 A232 I234
BS03 UDP B C1014 G1015 R1046 S1049 H1050 R1204 K1209 Y1275 N1277 E1306 Y1307 T1308 E1311 C17 G18 R49 S52 H53 R197 K202 Y268 N270 E299 Y300 T301 E304
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
PDBsum1y6g
PubMed16081100
UniProtP04519|GSTA_BPT4 DNA alpha-glucosyltransferase (Gene Name=agt)

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