Structure of PDB 1o0r Chain A

Receptor sequence
>1o0rA (length=271) Species: 9913 (Bos taurus) [Search protein sequence]
TACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPHK
VAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAKL
LNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKFG
FSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGMS
VSRPNAVIGKTRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYM
VLEVQRYPLYTKITVDIGTPS
3D structure
PDB1o0r CRYSTAL STRUCTURE OF BETA 1,4-GALACTOSYLTRANSFERASE COMPLEX WITH UDP-GAL REVEALS AN OLIGOSACCHARIDE ACCEPTOR BINDING SITE
ChainA
Resolution2.3 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 A P187 F188 R189 R191 F226 R228 D252 V253 D254 G292 W314 G315 E317 H347 D350 P56 F57 R58 R60 F95 R97 D121 V122 D123 G161 W183 G184 E186 H216 D219
BS02 MN A D254 M344 H347 D123 M213 H216
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:1o0r, PDBe:1o0r, PDBj:1o0r
PDBsum1o0r
PubMed12051854
UniProtP08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)

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