Structure of PDB 1nkh Chain B

Receptor sequence

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

LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPH
KVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAK
LLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKF
GFSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM
SVSRPNAVIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTY
MVLEVQRYPLYTKITVDIGTPS

3D structure

• PDB: 1nkh Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta-1,4-galactosyltransferase
• Chain: B
• 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	MN	B	D254 M344 H347	D124 M214 H217
BS02	UDP	B	P187 F188 R189 R191 F226 D252 V253 D254 W314 M344 H347 D350	P57 F58 R59 R61 F96 D122 V123 D124 W184 M214 H217 D220
BS03	UDP	B	L155 K156 E159 Q386 Y388 P389 L390	L25 K26 E29 Q256 Y258 P259 L260

Gene Ontology

Molecular Function

• GO:0016757 glycosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:1nkh, PDBe:1nkh, PDBj:1nkh
• PDBsum: 1nkh
• PubMed: 11419947
• UniProt: P08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)