Structure of PDB 1sxp Chain B

Receptor sequence
>1sxpB (length=351) Species: 10665 (Tequatrovirus T4) [Search protein sequence]
MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTD
IRLPFSQSWPNVKNRPWAYLYTEEELLIKSPIKVISQGINLDIAKAAHKK
VDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMV
EFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQA
IAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV
NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAID
L
3D structure
PDB1sxp Structural evidence of a passive base flipping mechanism for {beta}-Glucosyltransferase
ChainB
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 B S189 N215 K237 S189 N215 K237
BS02 dna B K16 R217 K219 Q220 G236 K237 K16 R217 K219 Q220 G236 K237
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:1sxp, PDBe:1sxp, PDBj:1sxp
PDBsum1sxp
PubMed15178685
UniProtP04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)

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