Structure of PDB 2agd Chain C

Receptor sequence

>2agdC (length=273) Species: 9606 (Homo sapiens)

SLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSP
HKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRA
KLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDK
FGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRG
MSISRPNAVVGTTRHIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLT
YQVLDVQRYPLYTQITVDIGTPS

3D structure

• PDB: 2agd Oligosaccharide Preferences of beta1,4-Galactosyltransferase-I: Crystal Structures of Met340His Mutant of Human beta1,4-Galactosyltransferase-I with a Pentasaccharide and Trisaccharides of the N-Glycan Moiety
• Chain: C
• Resolution: 1.9 Å

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	MN	C	D250 H340 H343	D125 H215 H218
BS02	UDH	C	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

Gene Ontology

Molecular Function

• GO:0016757 glycosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:2agd, PDBe:2agd, PDBj:2agd
• PDBsum: 2agd
• PubMed: 16157350
• UniProt: P15291|B4GT1_HUMAN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)