Structure of PDB 2fyb Chain A

Receptor sequence
>2fybA (length=272) Species: 9606 (Homo sapiens) [Search protein sequence]
GRGSASLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPR
DCVSPHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDT
IFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRCFSQPRHIS
VAMDKFGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNR
LVFRGMSISRPNAVVGTTRHIRHSPNPQRFDRIAHTKETMLSDGLNSLTY
QVLDVQRYPLYTQITVDIGTPS
3D structure
PDB2fyb Structural Snapshots of beta-1,4-Galactosyltransferase-I Along the Kinetic Pathway.
ChainA
Resolution1.9 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
Catalytic site (residue number reindexed from 1) D128 D130 W190 E193 D194 H220 H223
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 D130 H220 H223
BS02 UDP A P183 F184 R185 R187 F222 D248 V249 D250 H343 P63 F64 R65 R67 F102 D128 V129 D130 H223
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:2fyb, PDBe:2fyb, PDBj:2fyb
PDBsum2fyb
PubMed16497331
UniProtP15291|B4GT1_HUMAN Beta-1,4-galactosyltransferase 1 (Gene Name=B4GALT1)

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