Structure of PDB 2aes Chain A

Receptor sequence

>2aesA (length=272) Species: 9606 (Homo sapiens)

LPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPH
KVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAK
LLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKF
GFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRGM
SISRPNAVVGTTRHIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTY
QVLDVQRYPLYTQITVDIGTPS

3D structure

• PDB: 2aes 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: A
• Resolution: 2.0 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): D122 D124 W184 E187 D188 H214 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	MN	A	D250 H340 H343	D124 H214 H217
BS02	UDH	A	P183 F184 R185 R187 F222 D248 V249 D250 K275 W310 H340 H343 R345 D346	P57 F58 R59 R61 F96 D122 V123 D124 K149 W184 H214 H217 R219 D220

Gene Ontology

Molecular Function

• GO:0016757 glycosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

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