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BioLiP

Structure of PDB 2vsn Chain B Binding Site BS01

Receptor Information
>2vsn Chain B (length=534) Species: 314565 (Xanthomonas campestris pv. campestris str. 8004) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VAWLMLADAELGAGEMAVQRGLPEAVARLGRVRWTQQRHAEAAVLLQQAS
DAAPEHPGIALWLGHALEDAGQAEAAAAAYTRAHQLLPEEPYITAQLLNW
RRRLCDWRALDVLSAQVRAAVAQGVGAVEPFAFLSEDASAAEQLACARTR
AQAIAASVRPLAPTRVRSKGPLRVGFVSNGFGAHPTGLLTVALFEALQRR
QPDLQMHLFATSGDDGSTLRTRLAQASTLHDVTALGHLATAKHIRHHGID
LLFDLAGWGGGGRPEVFALRPAPVQVNWLAYPGTSGAPWMDYVLGDAFAL
PPALEPFYSEHVLRLQGAFQPSDTSRVVAEPPSRTQCGLPEQGVVLCCFN
NSYKLNPQSMARMLAVLREVPDSVLWLLSGPGEADARLRAFAHAQGVDAQ
RLVFMPKLPHPQYLARYRHADLFLDTHPYNAHTTASDALWTGCPVLTTPG
ETFAARVAGSLNHHLGLDEMNVADDAAFVAKAVALASDPAALTALHARVD
VLRRASGVFHMDGFADDFGALLQALARRHGWLGI
Ligand information
Ligand IDUDP
InChIInChI=1S/C9H14N2O12P2/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(22-8)3-21-25(19,20)23-24(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
InChIKeyXCCTYIAWTASOJW-XVFCMESISA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)OP(=O)(O)O)O)O
CACTVS 3.370O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
CACTVS 3.370O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)O)O)O
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O
FormulaC9 H14 N2 O12 P2
NameURIDINE-5'-DIPHOSPHATE
ChEMBLCHEMBL130266
DrugBankDB03435
ZINCZINC000004490939
PDB chain2vsn Chain B Residue 900 [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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PDB2vsn Structure of an O-Glcnac Transferase Homolog Provides Insight Into Intracellular Glycosylation.
Resolution2.75 Å
Binding residue
(original residue number in PDB)		L222 K388 K441 L442 H444 Y447 H466 T467 T468 D471
Binding residue
(residue number reindexed from 1)		L188 K354 K407 L408 H410 Y413 H432 T433 T434 D437
Annotation score4
Enzymatic activity
Enzyme Commision number 2.4.-.-
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016757 glycosyltransferase activity

View graph for
Molecular Function
External links

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