Structure of PDB 2vfz Chain B Binding Site BS01

Receptor Information
>2vfz Chain B (length=281) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGLT
VFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPLR
SFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQD
KFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHAA
IFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTKI
LSPEYCWDYHIGLPADIKLVKMSWQTKEYNV
Ligand information
Ligand IDUPF
InChIInChI=1S/C15H23FN2O16P2/c16-8-11(23)9(21)5(3-19)32-14(8)33-36(28,29)34-35(26,27)30-4-6-10(22)12(24)13(31-6)18-2-1-7(20)17-15(18)25/h1-2,5-6,8-14,19,21-24H,3-4H2,(H,26,27)(H,28,29)(H,17,20,25)/t5-,6-,8-,9+,10-,11-,12-,13-,14-/m1/s1
InChIKeyNGTCPFGWXMBZEP-KBQKSTHMSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC[C@H]1O[C@H](O[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)[C@H](F)[C@@H](O)[C@H]1O
ACDLabs 10.04O=P(OC1OC(C(O)C(O)C1F)CO)(O)OP(=O)(O)OCC3OC(N2C=CC(=O)NC2=O)C(O)C3O
OpenEye OEToolkits 1.5.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OC3C(C(C(C(O3)CO)O)O)F)O)O
OpenEye OEToolkits 1.5.0C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)O[P@@](=O)(O)O[C@@H]3[C@@H]([C@H]([C@H]([C@H](O3)CO)O)O)F)O)O
CACTVS 3.341OC[CH]1O[CH](O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O)[CH](F)[CH](O)[CH]1O
FormulaC15 H23 F N2 O16 P2
NameURIDINE-5'-DIPHOSPHATE-2-DEOXY-2-FLUOROGALACTOSE;
URIDINE-5'-MONOPHOSPHATE 2-DEOXY-2-FLUORO-GALACTOPYRANOSYL-MONOPHOSPHATE ESTER
ChEMBL
DrugBankDB02976
ZINCZINC000015553713
PDB chain2vfz Chain B Residue 2364 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2vfz Conformational Changes Induced by Binding Udp-2F-Galactose to Alpha-1,3 Galactosyltransferase-Implications for Catalysis
Resolution2.4 Å
Binding residue
(original residue number in PDB)		F1134 A1135 V1136 Y1139 W1195 I1198 S1199 R1202 D1225 V1226 D1227 H1280 A1281 A1282 H1315 D1316 E1317 K1359
Binding residue
(residue number reindexed from 1)		F52 A53 V54 Y57 W113 I116 S117 R120 D143 V144 D145 H198 A199 A200 H233 D234 E235 K277
Annotation score3
Binding affinityMOAD: Ki=245uM
Enzymatic activity
Catalytic site (original residue number in PDB) Q1247 H1280 W1314 E1317 W1356
Catalytic site (residue number reindexed from 1) Q165 H198 W232 E235 W274
Enzyme Commision number 2.4.1.87: N-acetyllactosaminide 3-alpha-galactosyltransferase.
Gene Ontology
Molecular Function
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vfz, PDBe:2vfz, PDBj:2vfz
PDBsum2vfz
PubMed17493636
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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