Structure of PDB 3wy3 Chain A

Receptor sequence
>3wy3A (length=535) Species: 1076127 (Halomonas sp. H11) [Search protein sequence]
NMMWWRGGVIYQIYPRSFLDSRGDGVGDLNGITEKLDYVASLNVDGIWLS
PFFTSPMLDFGYDVSDYRDVDPMFGTLEDFKALLEKAHSLGLKVMIDQVI
SHTSDQHPWFQESRQNRTNPKADWFVWADPKPDGTPPNNWLSIFGGSAWT
FDSRRQQYYLHNFLTSQPDVNFHHPEARQAQLDNMRFWLDLGVDGFRLNT
VNFYFHDAELRDNPPVPKGEAKTLGAPEANPYTWQRHVYDLSRPENLDFL
KDLRALMDEYPGTTTVGEIGDDNPLERMAEYTAGGDKLHMAYTFDLLNMP
HSASYLREVIERFQRLAGDAWPCWATSNHDVVRSATRWGADEDPHAYPKV
MLAVLFSLRGSVCLYQGEELGLPEADVPFERIQDPYGKVLWPEFKGRDGC
RTPMPWTDGEQGGFSPVEPWLPMEARHLELAVSRQQDDPNATLNTVRALL
AFRRSHPALFDGDLSLVDVGDDLLGFTRQKGDETLLCVFNLTGQEQQTTL
PVEVASDLPVAHFTATRDGSTLTLPAYQAAFMQVA
3D structure
PDB3wy3 Structural analysis of the alpha-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D100 R200 N202 E271 H332 D333
Catalytic site (residue number reindexed from 1) D97 R197 N199 E268 H329 D330
Enzyme Commision number 3.2.1.20: alpha-glucosidase.
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 MG A D27 V29 D31 D24 V26 D28
BS02 GOL A N165 D172 V173 F206 Y207 H209 N162 D169 V170 F203 Y204 H206
BS03 GOL A F166 E271 F163 E268
BS04 BGC A D62 Y65 F166 N202 E271 H332 D333 R400 D59 Y62 F163 N199 E268 H329 D330 R397
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0004558 alpha-1,4-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3wy3, PDBe:3wy3, PDBj:3wy3
PDBsum3wy3
PubMed26057678
UniProtH3K096

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