Structure of PDB 1ixy Chain A

Receptor sequence
>1ixyA (length=351) Species: 10665 (Tequatrovirus T4) [Search protein sequence]
MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTD
IRLPFSQSWPNVKNRPWAYLYTEEELLIKSPIKVISQGINLDIAKAAHKK
VDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMV
EFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQA
IAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV
NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAID
L
3D structure
PDB1ixy A Base-flipping Mechanism for the T4 Phage beta-Glucosyltransferase and Identification of a Transition-state Analog
ChainA
Resolution2.5 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 F72 D100 R191
Catalytic site (residue number reindexed from 1) E22 F72 D100 R191
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 dna A T17 S68 N70 F72 S189 S192 N215 T17 S68 N70 F72 S189 S192 N215
BS02 dna A N70 F71 F72 G73 G74 R115 K150 R217 N70 F71 F72 G73 G74 R115 K150 R217
BS03 UDP A V18 G188 R191 R195 G214 K237 I238 M240 V243 R269 E272 V18 G188 R191 R195 G214 K237 I238 M240 V243 R269 E272
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
PDBsum1ixy
PubMed12445783
UniProtP04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)

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