Structure of PDB 3ee5 Chain B

Receptor sequence
>3ee5B (length=273) Species: 9606 (Homo sapiens) [Search protein sequence]
SLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSP
HKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRA
KLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDK
FGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRG
MSISRPNAVVGTTRHIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLT
YQVLDVQRYPLYTQITVDIGTPS
3D structure
PDB3ee5 Deoxygenated Disaccharide Analogs as Specific Inhibitors of {beta}1-4-Galactosyltransferase 1 and Selectin-mediated Tumor Metastasis
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D248 D250 W310 E313 D314 H340 H343 R345
Catalytic site (residue number reindexed from 1) D123 D125 W185 E188 D189 H215 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 UDH B P183 F184 R185 R187 F222 D248 V249 D250 K275 W310 H343 R345 D346 P58 F59 R60 R62 F97 D123 V124 D125 K150 W185 H218 R220 D221
BS02 MN B D250 H340 H343 D125 H215 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:3ee5, PDBe:3ee5, PDBj:3ee5
PDBsum3ee5
PubMed19106107
UniProtP15291|B4GT1_HUMAN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)

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