Structure of PDB 4krv Chain A

Receptor sequence

>4krvA (length=272) Species: 9913 (Bos taurus)

LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPH
KVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAK
LLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKF
GFSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM
SVSRPNAVIGKTRHIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTY
MVLEVQRYPLYTKITVDIGTPS

3D structure

• PDB: 4krv Investigations on beta 1,4-galactosyltransferase I using 6-sulfo-GlcNAc as an acceptor sugar substrate.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D252 D254 W314 E317 D318 H344 H347 R349
• Catalytic site (residue number reindexed from 1): D122 D124 W184 E187 D188 H214 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	MN	A	D254 H344 H347	D124 H214 H217
BS02	UDH	A	P187 F188 R189 R191 F226 D252 V253 D254 W314 H344 H347 R349 D350 N353	P57 F58 R59 R61 F96 D122 V123 D124 W184 H214 H217 R219 D220 N223
BS03	NGS	A	F280 Y286 Y289 W314 G315 G316 D318 R359	F150 Y156 Y159 W184 G185 G186 D188 R229
BS04	SO4	A	D175 Q210	D45 Q80
BS05	SO4	A	R265 F267 S268	R135 F137 S138
BS06	SO4	A	S224 M225 K352 P401	S94 M95 K222 P271

Gene Ontology

Molecular Function

• GO:0016757 glycosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:4krv, PDBe:4krv, PDBj:4krv
• PDBsum: 4krv
• PubMed: 23942731
• UniProt: P08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)