Structure of PDB 1euu Chain A

Receptor sequence
>1euuA (length=601) Species: 1881 (Micromonospora viridifaciens) [Search protein sequence]
GEPLYTEQDLAVNGREGFPNYRIPALTVTPDGDLLASYDGRPTGIDAPGP
NSILQRRSTDGGRTWGEQQVVSAGQTTAPIKGFSDPSYLVDRETGTIFNF
HVYSQRQGFAGSRPGTDPADPNVLHANVATSTDGGLTWSHRTITADITPD
PGWRSRFAASGEGIQLRYGPHAGRLIQQYTIINAAGAFQAVSVYSDDHGR
TWRAGEAVGVGMDENKTVELSDGRVLLNSRDSARSGYRKVAVSTDGGHSY
GPVTIDRDLPDPTNNASIIRAFPDAPAGSARAKVLLFSNAASQTSRSQGT
IRMSCDDGQTWPVSKVFQPGSMSYSTLTALPDGTYGLLYEPGTGIRYANF
NLAWLGGICAPFTIPDVALEPGQQVTVPVAVTNQSGIAVPKPSLQLDASP
DWQVQGSVEPLMPGRQAKGQVTITVPAGTTPGRYRVGATLRTSAGNASTT
FTVTVGLLDQARMSIADVDSEETAREDGRASNVIDGNPSTFWHTEWSRAD
APGYPHRISLDLGGTHTISGLQYTRRQNSANEQVADYEIYTSLNGTTWDG
PVASGRFTTSLAPQRAVFPARDARYIRLVALSEQTGHKYAAVAELEVEGQ
R
3D structure
PDB1euu The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D92 E260 Y370
Catalytic site (residue number reindexed from 1) D46 E214 Y324
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 GAL A W542 R572 W496 R526
Gene Ontology
Molecular Function
GO:0004308 exo-alpha-sialidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006689 ganglioside catabolic process
GO:0009313 oligosaccharide catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1euu, PDBe:1euu, PDBj:1euu
PDBsum1euu
PubMed8591030
UniProtQ02834|NANH_MICVI Sialidase (Gene Name=nedA)

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