BioLiP

Receptor Information

>4nc5 Chain A (length=354) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRAAELIVLRRGD
YDAPTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFFIAIPGQ
VRANVTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQ
LNDRARSLVVPAYAYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDT
LECQVAEVETQRVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPP
PQGCQGSVISFPSPRAQWLLYTHPTHSWQRADLGAYLNPRPPAPEAWSEP
VLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYEEIVFLMFTLKQAFP
AEYL

Ligand ID

FSI

InChI

InChI=1S/C11H18FNO9/c1-3(15)13-5-7(18)9(12)11(21,10(19)20)22-8(5)6(17)4(16)2-14/h4-9,14,16-18,21H,2H2,1H3,(H,13,15)(H,19,20)/t4-,5-,6-,7-,8-,9-,11+/m1/s1

InChIKey

ALJLGESFXXDPKH-RISWTRDCSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.7.6	CC(=O)N[C@@H]1[C@H]([C@H]([C@](O[C@H]1[C@@H]([C@@H](CO)O)O)(C(=O)O)O)F)O
OpenEye OEToolkits 1.7.6	CC(=O)NC1C(C(C(OC1C(C(CO)O)O)(C(=O)O)O)F)O
CACTVS 3.370	CC(=O)N[CH]1[CH](O)[CH](F)[C](O)(O[CH]1[CH](O)[CH](O)CO)C(O)=O
ACDLabs 12.01	O=C(O)C1(O)OC(C(NC(=O)C)C(O)C1F)C(O)C(O)CO
CACTVS 3.370	CC(=O)N[C@@H]1[C@@H](O)[C@@H](F)[C@](O)(O[C@H]1[C@H](O)[C@H](O)CO)C(O)=O

Formula

C11 H18 F N O9

Name

5-acetamido-3,5-dideoxy-3-fluoro-D-erythro-alpha-L-manno-non-2-ulopyranosonic acid;
5-(acetylamino)-3,5-dideoxy-3-fluoro-D-erythro-alpha-L-manno-non-2-ulopyranosonic acid;
3-FLUOROSIALIC ACID;
5-acetamido-3,5-dideoxy-3-fluoro-D-erythro-alpha-L-manno-non-2-ulosonic acid;
5-acetamido-3,5-dideoxy-3-fluoro-D-erythro-L-manno-non-2-ulosonic acid;
5-acetamido-3,5-dideoxy-3-fluoro-D-erythro-manno-non-2-ulosonic acid

PDB chain

4nc5 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	4nc5 Tuning mechanism-based inactivators of neuraminidases: mechanistic and structural insights.
Resolution	2.513 Å
Binding residue (original residue number in PDB)	R21 Y181 L217 E218 R237 R304 Y334
Binding residue (residue number reindexed from 1)	R19 Y165 L201 E202 R219 R280 Y310
Annotation score	2

Catalytic site (original residue number in PDB)	E218
Catalytic site (residue number reindexed from 1)	E202
Enzyme Commision number	3.2.1.18: exo-alpha-sialidase.

	Molecular Function
GO:0004308	exo-alpha-sialidase activity
GO:0005515	protein binding
GO:0016798	hydrolase activity, acting on glycosyl bonds

	Biological Process
GO:0006516	glycoprotein catabolic process
GO:0006689	ganglioside catabolic process
GO:0009313	oligosaccharide catabolic process
GO:0016042	lipid catabolic process
GO:0046479	glycosphingolipid catabolic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005764	lysosome
GO:0005829	cytosol
GO:0016020	membrane
GO:1902494	catalytic complex

PDB	RCSB:4nc5, PDBe:4nc5, PDBj:4nc5
PDBsum	4nc5
PubMed	24591206
UniProt	Q9Y3R4\|NEUR2_HUMAN Sialidase-2 (Gene Name=NEU2)

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Structure of PDB 4nc5 Chain A Binding Site BS01