Structure of PDB 3wy4 Chain A

Receptor sequence
>3wy4A (length=535) Species: 1076127 (Halomonas sp. H11) [Search protein sequence]
NMMWWRGGVIYQIYPRSFLDSRGDGVGDLNGITEKLDYVASLNVDGIWLS
PFFTSPMLDFGYDVSDYRDVDPMFGTLEDFKALLEKAHSLGLKVMIDQVI
SHTSDQHPWFQESRQNRTNPKADWFVWADPKPDGTPPNNWLSIFGGSAWT
FDSRRQQYYLHNFLTSQPDVNFHHPEARQAQLDNMRFWLDLGVDGFRLDT
VNFYFHDAELRDNPPVPKGEAKTLGAPEANPYTWQRHVYDLSRPENLDFL
KDLRALMDEYPGTTTVGQIGDDNPLERMAEYTAGGDKLHMAYTFDLLNMP
HSASYLREVIERFQRLAGDAWPCWATSNHDVVRSATRWGADEDPHAYPKV
MLAVLFSLRGSVCLYQGEELGLPEADVPFERIQDPYGKVLWPEFKGRDGC
RTPMPWTDGEQGGFSPVEPWLPMEARHLELAVSRQQDDPNATLNTVRALL
AFRRSHPALFDGDLSLVDVGDDLLGFTRQKGDETLLCVFNLTGQEQQTTL
PVEVASDLPVAHFTATRDGSTLTLPAYQAAFMQVA
3D structure
PDB3wy4 Structural analysis of the alpha-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism
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) D100 R200 D202 Q271 H332 D333
Catalytic site (residue number reindexed from 1) D97 R197 D199 Q268 H329 D330
Enzyme Commision number 3.2.1.20: alpha-glucosidase.
Interaction with ligand
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
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Biological Process
External links
PDB RCSB:3wy4, PDBe:3wy4, PDBj:3wy4
PDBsum3wy4
PubMed26057678
UniProtH3K096

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