Structure of PDB 2am4 Chain A Binding Site BS01

Receptor Information
>2am4 Chain A (length=342) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQVIA
SYGSAVTHIRQPDLSNIAVQPDHRKFQGYYKIARHYRWALGQIFHNFNYP
AAVVVEDDLEVAPDFFEYFQATYPLLKADPSLWCVSAWNDNGKEQMVDSS
KPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRKGRAC
VRPEISRTMTFGRKGVSHGQFFDQHLKFIKLNQQFVPFTQLDLSYLQQEA
YDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFAKALGV
MDDLKSGVPRAGYRGIVTFLFRGRRVHLAPPQTWDGYDPSWT
Ligand information
Ligand IDU2F
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-NQQHDEILSA-N
SMILES
SoftwareSMILES
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
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
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-FLUORO-ALPHA-D-GLUCOSE
ChEMBLCHEMBL593830
DrugBankDB03488
ZINCZINC000016051573
PDB chain2am4 Chain A Residue 449 [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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PDB2am4 X-ray Crystal Structures of Rabbit N-acetylglucosaminyltransferase I (GnT I) in Complex with Donor Substrate Analogues.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		I113 A114 C115 R117 D144 C145 Y184 I187 H190 E211 D212 D291 G320 V321 S322
Binding residue
(residue number reindexed from 1)		I8 A9 C10 R12 D39 C40 Y79 I82 H85 E106 D107 D186 G215 V216 S217
Annotation score3
Binding affinityMOAD: Ki=190uM
PDBbind-CN: -logKd/Ki=3.72,Ki=190uM
Enzymatic activity
Catalytic site (original residue number in PDB) D213 D291
Catalytic site (residue number reindexed from 1) D108 D186
Enzyme Commision number 2.4.1.101: alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase.
Gene Ontology
Molecular Function
GO:0008375 acetylglucosaminyltransferase activity
Biological Process
GO:0006486 protein glycosylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2am4, PDBe:2am4, PDBj:2am4
PDBsum2am4
PubMed16769084
UniProtP27115|MGAT1_RABIT Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (Gene Name=MGAT1)

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