Structure of PDB 2vs4 Chain B

Receptor sequence
>2vs4B (length=288) Species: 9913 (Bos taurus) [Search protein sequence]
SKLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVG
LTVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGP
LRSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVF
QDKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYH
AAIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHEESHLNKYFLLNKPT
KILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNNV
3D structure
PDB2vs4 Structural Basis of Udp-Galactose Binding by Alpha- 1,3-Galactosyltransferase (Alpha3Gt): Role of Negative Charge on Aspartic Acid 316 in Structure and Activity.
ChainB
Resolution1.77 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) Q247 H280 W314 E317 W356 R365
Catalytic site (residue number reindexed from 1) Q167 H200 W234 E237 W276 R285
Enzyme Commision number 2.4.1.87: N-acetyllactosaminide 3-alpha-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 GAL B Q247 T259 W314 E317 W356 Q167 T179 W234 E237 W276
BS02 MN B D225 D227 D145 D147
BS03 UDP B F134 A135 V136 Y139 I198 R202 D225 V226 D227 K359 Y361 R365 F54 A55 V56 Y59 I118 R122 D145 V146 D147 K279 Y281 R285
Gene Ontology
Molecular Function
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2vs4, PDBe:2vs4, PDBj:2vs4
PDBsum2vs4
PubMed18651752
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

[Back to BioLiP]