Structure of PDB 1sxq Chain A

Receptor sequence

>1sxqA (length=351) Species: 10665 (Tequatrovirus T4)

MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTD
IRLPFSQSWPNVKNRPWAYLYTEEELLIKSPIKVISQGINLDIAKAAHKK
VDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMV
EFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQA
IAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV
NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAID
L

3D structure

• PDB: 1sxq Structural evidence of a passive base flipping mechanism for {beta}-Glucosyltransferase
• Chain: A
• Resolution: 1.8 Å

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	S68 F72 S192 N215 R217 K237	S68 F72 S192 N215 R217 K237
BS02	dna	A	G73 G74 K75 P116 W117 Y119 R217 K219	G73 G74 K75 P116 W117 Y119 R217 K219
BS03	UDP	A	V18 G188 S189 R191 R195 F213 G214 K237 I238 M240 V243 R269 E272	V18 G188 S189 R191 R195 F213 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

External links

• PDB: RCSB:1sxq, PDBe:1sxq, PDBj:1sxq
• PDBsum: 1sxq
• PubMed: 15178685
• UniProt: P04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)