Structure of PDB 1o23 Chain D

Receptor sequence
>1o23D (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.
ChainD
Resolution2.32 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D654 D656 W716 E719 D720 M746 H749 R751
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 D D656 M746 H749 D124 M214 H217
BS02 UPG D P589 F590 R591 R593 F628 R630 D654 V655 D656 G694 W716 G717 E719 D720 M746 H749 D752 P57 F58 R59 R61 F96 R98 D122 V123 D124 G162 W184 G185 E187 D188 M214 H217 D220
BS03 UDP D L557 Y790 P791 L792 L25 Y258 P259 L260
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function

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

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