Structure of PDB 1fr8 Chain B

Receptor sequence
>1fr8B (length=271) Species: 9913 (Bos taurus) [Search protein sequence]
TACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPHK
VAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAKL
LNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKFG
FSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGMS
VSRPNAVIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYM
VLEVQRYPLYTKITVDIGTPS
3D structure
PDB1fr8 Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D252 D254 W314 E317 D318 M344 H347 R349
Catalytic site (residue number reindexed from 1) D121 D123 W183 E186 D187 M213 H216 R218
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 GDU B P187 F188 R189 R191 F226 D252 V253 D254 P56 F57 R58 R60 F95 D121 V122 D123
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:1fr8, PDBe:1fr8, PDBj:1fr8
PDBsum1fr8
PubMed10393171
UniProtP08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)

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