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BioLiP

Structure of PDB 5xvs Chain A Binding Site BS01

Receptor Information
>5xvs Chain A (length=359) Species: 470 (Acinetobacter baumannii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKKIAVFTGTRAEYGLLYWLMRDIQQDPELELQILATAMHYSPEHGETWK
TIVKDGFEITESVEMLLSSDTSSAVVKSMGVGLLGFADALKRMQPDVLVV
LGDRFEALAVTQAALIMHVPVAHLHGGEITEGAYDESIRHAITKMSNIHF
AAAEEYKKRIIQLGEQPERVFNVGALGLDHIQRTTFKSISELSELYDFDF
SKPYFLITYHPENVAPLFDALKQINDVNFIFSYPNTNIVKAMLDLKAQLP
DRVLLVKSFGIQNYLSVLKNALAMVGNSSSGLSEAPALQVPTVNIGDRQK
GRLRCESILDVRLDENEIVEALQKAINFPPLGLGNTSQKIIEVIKTTDFK
KKAPFYDLL
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 chain5xvs Chain A Residue 402 [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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PDB5xvs The tetrameric structure of sialic acid-synthesizing UDP-GlcNAc 2-epimerase fromAcinetobacter baumannii: A comparative study with human GNE.
Resolution2.383 Å
Binding residue
(original residue number in PDB)		H210 F270 Y275 S289 S290 S291 E295 R309
Binding residue
(residue number reindexed from 1)		H210 F259 Y264 S278 S279 S280 E284 R298
Annotation score3
Enzymatic activity
Enzyme Commision number 3.2.1.183: UDP-N-acetylglucosamine 2-epimerase (hydrolyzing).
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008761 UDP-N-acetylglucosamine 2-epimerase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0102388 UDP-N,N'-diacetylbacillosamine 2-epimerase activity
Biological Process
GO:0006047 UDP-N-acetylglucosamine metabolic process

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Molecular Function
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Biological Process
External links

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