Structure of PDB 1nf5 Chain D

Receptor sequence
>1nf5D (length=272) Species: 9913 (Bos taurus) [Search protein sequence]
LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPH
KVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAK
LLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKF
GFSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM
SVSRPNAVIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTY
MVLEVQRYPLYTKITVDIGTPS
3D structure
PDB1nf5 Crystal Structure of Lactose Synthase Reveals a Large Conformational Change in its Catalytic Component, the beta-1,4-galactosyltransferase
ChainD
Resolution2.0 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) 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 BGC D F280 Y286 Y289 G315 G316 D318 D319 F150 Y156 Y159 G185 G186 D188 D189
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:1nf5, PDBe:1nf5, PDBj:1nf5
PDBsum1nf5
PubMed11419947
UniProtP08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)

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