Structure of PDB 2fyd Chain D

Receptor sequence

>2fydD (length=272) Species: 9913 (Bos taurus)

LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPH
KVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAK
LLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKF
GFSLPYVQYFGGVSALSKQQFLSINGFPNNYCGWGGEDDDIYNRLAFRGM
SVSRPNAVIGKTRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTY
MVLEVQRYPLYTKITVDIGTCS

3D structure

• PDB: 2fyd Structural Snapshots of beta-1,4-Galactosyltransferase-I Along the Kinetic Pathway.
• Chain: D
• Resolution: 2.0 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	BGC	D	Y286 Y289 G316 D318 D319	Y156 Y159 G186 D188 D189
BS02	MN	D	D254 M344 H347	D124 M214 H217
BS03	UDP	D	P187 F188 R189 R191 F226 D252 V253 D254 W314 M344 H347 D350	P57 F58 R59 R61 F96 D122 V123 D124 W184 M214 H217 D220

Gene Ontology

Molecular Function

• GO:0016757 glycosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:2fyd, PDBe:2fyd, PDBj:2fyd
• PDBsum: 2fyd
• PubMed: 16497331
• UniProt: P08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)