Structure of PDB 1m5r Chain A

Receptor sequence

>1m5rA (length=351) Species: 10665 (Tequatrovirus T4)

MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKS
FDEVDVNDYDRLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTD
IRLPFSQSWPNVKNRPWAYLYTEEELLIKSPIKVISQGINLDIAKAAHKK
VDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMV
EFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQA
IAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV
NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAID
L

3D structure

• PDB: 1m5r A Base-flipping mechanism for the T4 phage beta-glucosyltransferase and identification of a transition state analog
• 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	T17 S68 N70 F72 R102 S192 N215 K222 K237	T17 S68 N70 F72 R102 S192 N215 K222 K237
BS02	dna	A	N70 F71 F72 G73 G74 K75 R115	N70 F71 F72 G73 G74 K75 R115
BS03	UDP	A	V18 G187 G188 R191 R195 F213 G214 K237 I238 M240 V243 R269 E272	V18 G187 G188 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:1m5r, PDBe:1m5r, PDBj:1m5r
• PDBsum: 1m5r
• PubMed: 12445783
• UniProt: P04547|GSTB_BPT4 DNA beta-glucosyltransferase (Gene Name=bgt)