Structure of PDB 1yro Chain B

Receptor sequence

>1yroB (length=272) Species: 9913 (Bos taurus)

LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPH
KVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNKAK
LLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKF
GFSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM
SVSRPNAVIGKTRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTY
MVLEVQRYPLYTKITVDIGTPS

3D structure

• PDB: 1yro Mutation of Arginine 228 to Lysine Enhances the Glucosyltransferase Activity of Bovine beta-1,4-Galactosyltransferase I
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D252 D254 W314 E317 D318 M344 H347 R349
• Catalytic site (residue number reindexed from 1): D122 D124 W184 E187 D188 M214 H217 R219
• Enzyme Commision number: 2.4.1.-
  2.4.1.22: lactose synthase.
  2.4.1.275: neolactotriaosylceramide beta-1,4-galactosyltransferase.
  2.4.1.38: beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase.
  2.4.1.90: N-acetyllactosamine synthase.

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	GDU	B	P187 F188 R189 R191 F226 K228 D252 V253 D254 G292 W314 G315 E317 D318 H347 R349 D350	P57 F58 R59 R61 F96 K98 D122 V123 D124 G162 W184 G185 E187 D188 H217 R219 D220
BS02	MN	B	D254 M344 H347	D124 M214 H217
BS03	UDP	B	L155 E159 Q192 Y388 P389 L390 Y391	L25 E29 Q62 Y258 P259 L260 Y261

Gene Ontology

Molecular Function

• GO:0016757 glycosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:1yro, PDBe:1yro, PDBj:1yro
• PDBsum: 1yro
• PubMed: 15736931
• UniProt: P08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)