Structure of PDB 1o0r Chain B

Receptor sequence
>1o0rB (length=273) Species: 9913 (Bos taurus) [Search protein sequence]
SLTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISP
HKVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRA
KLLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDK
FGFSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRG
MSVSRPNAVIGKTRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLT
YMVLEVQRYPLYTKITVDIGTPS
3D structure
PDB1o0r CRYSTAL STRUCTURE OF BETA 1,4-GALACTOSYLTRANSFERASE COMPLEX WITH UDP-GAL REVEALS AN OLIGOSACCHARIDE ACCEPTOR BINDING SITE
ChainB
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) D123 D125 W185 E188 D189 M215 H218 R220
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 R228 D252 V253 D254 K279 G292 W314 G315 E317 H347 D350 P58 F59 R60 R62 F97 R99 D123 V124 D125 K150 G163 W185 G186 E188 H218 D221
BS02 MN B D254 M344 H347 D125 M215 H218
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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