Structure of PDB 1pzy Chain D

Receptor sequence
>1pzyD (length=271) Species: 9913 (Bos taurus) [Search protein sequence]
TACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPHK
VAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAKL
LNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKFG
FSLPYVQYFGGVSALSKQQFLSINGFPNNYWGAGGEDDDIYNRLAFRGMS
VSRPNAVIGKTRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYM
VLEVQRYPLYTKITVDIGTPS
3D structure
PDB1pzy The Role of Tryptophan 314 in the Conformational Changes of beta 1,4-Galactosyltransferase-I
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D252 D254 A314 E317 D318 M344 H347 R349
Catalytic site (residue number reindexed from 1) D121 D123 A183 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 MN D D254 H347 D123 H216
BS02 UDP D P187 F188 R189 R191 F226 D252 V253 D254 D350 P56 F57 R58 R60 F95 D121 V122 D123 D219
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1pzy, PDBe:1pzy, PDBj:1pzy
PDBsum1pzy
PubMed12927542
UniProtP08037|B4GT1_BOVIN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)

[Back to BioLiP]