Structure of PDB 4irq Chain C

Receptor sequence
>4irqC (length=249) Species: 9606 (Homo sapiens) [Search protein sequence]
DIPEHWEEDASWGPHRLAVLVPFRERFEELLVFVPHMRRFLSRKKIRHHI
YVLNQVDHFRFNRAALINVGFLESSNSTDYIAMHDVDLLPLNEELDYGFP
EAGPFHVASPELHPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGRED
DEFYRRIKGAGLQLFRPSGITTGYKTFRHLHDPAWRKRDQKRIAAQKQEQ
FKVDREGGLNTVKYHVASRTALSVGGAPCTVLNIMLDCDKTATPWCTFS
3D structure
PDB4irq Crystal structures of beta-1,4-galactosyltransferase 7 enzyme reveal conformational changes and substrate binding.
ChainC
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) D163 D165 W224 E227 D228 T254 H257 H259
Catalytic site (residue number reindexed from 1) D85 D87 W146 E149 D150 T176 H179 H181
Enzyme Commision number 2.4.1.-
2.4.1.133: xylosylprotein 4-beta-galactosyltransferase.
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 D165 H257 H259 D87 H179 H181
BS02 UDP C P100 F101 R102 R104 F139 D163 V164 D165 Y194 H257 H259 R266 P22 F23 R24 R26 F61 D85 V86 D87 Y116 H179 H181 R188
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:4irq, PDBe:4irq, PDBj:4irq
PDBsum4irq
PubMed24052259
UniProtQ9UBV7|B4GT7_HUMAN Beta-1,4-galactosyltransferase 7 (Gene Name=B4GALT7)

[Back to BioLiP]