Structure of PDB 4nc5 Chain A

Receptor sequence
>4nc5A (length=354) Species: 9606 (Homo sapiens) [Search protein sequence]
SLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRAAELIVLRRGD
YDAPTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFFIAIPGQ
VRANVTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQ
LNDRARSLVVPAYAYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDT
LECQVAEVETQRVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPP
PQGCQGSVISFPSPRAQWLLYTHPTHSWQRADLGAYLNPRPPAPEAWSEP
VLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYEEIVFLMFTLKQAFP
AEYL
3D structure
PDB4nc5 Tuning mechanism-based inactivators of neuraminidases: mechanistic and structural insights.
ChainA
Resolution2.513 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FSI A R21 Y181 L217 E218 R237 R304 Y334 R19 Y165 L201 E202 R219 R280 Y310
Gene Ontology
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4nc5, PDBe:4nc5, PDBj:4nc5
PDBsum4nc5
PubMed24591206
UniProtQ9Y3R4|NEUR2_HUMAN Sialidase-2 (Gene Name=NEU2)

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