Structure of PDB 1o23 Chain B

Receptor sequence
>1o23B (length=272) Species: 9913 (Bos taurus) [Search protein sequence]
LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPH
KVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAK
LLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKF
GFSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM
SVSRPNAVIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTY
MVLEVQRYPLYTKITVDIGTPS
3D structure
PDB1o23 Alpha-Lactalbumin (La) Stimulates Milk Beta-1,4-Galactosyltransferase I (Beta 4Gal-T1) to Transfer Glucose from Udp-Glucose to N-Acetylglucosamine. Crystal Structure of Beta 4Gal-T1 X La Complex with Udp-Glc.
ChainB
Resolution2.32 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1o23, PDBe:1o23, PDBj:1o23
PDBsum1o23
PubMed11485999
UniProtP08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)

[Back to BioLiP]