Structure of PDB 1sxp Chain A

Receptor sequence
>1sxpA (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
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 P19 E22 S68 N70 F72 R102 T17 P19 E22 S68 N70 F72 R102
BS02 dna A N70 F71 F72 G73 G74 K75 R115 K150 K237 N70 F71 F72 G73 G74 K75 R115 K150 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1sxp, PDBe:1sxp, PDBj:1sxp
PDBsum1sxp
PubMed15178685
UniProtP04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)

[Back to BioLiP]