Structure of PDB 3wy2 Chain A

Receptor sequence
>3wy2A (length=535) Species: 1076127 (Halomonas sp. H11) [Search protein sequence]
NMMWWRGGVIYQIYPRSFLDSRGDGVGDLNGITEKLDYVASLNVDGIWLS
PFFTSPMLDFGYDVSDYRDVDPMFGTLEDFKALLEKAHSLGLKVMIDQVI
SHTSDQHPWFQESRQNRTNPKADWFVWADPKPDGTPPNNWLSIFGGSAWT
FDSRRQQYYLHNFLTSQPDVNFHHPEARQAQLDNMRFWLDLGVDGFRLDT
VNFYFHDAELRDNPPVPKGEAKTLGAPEANPYTWQRHVYDLSRPENLDFL
KDLRALMDEYPGTTTVGEIGDDNPLERMAEYTAGGDKLHMAYTFDLLNMP
HSASYLREVIERFQRLAGDAWPCWATSNHDVVRSATRWGADEDPHAYPKV
MLAVLFSLRGSVCLYQGEELGLPEADVPFERIQDPYGKVLWPEFKGRDGC
RTPMPWTDGEQGGFSPVEPWLPMEARHLELAVSRQQDDPNATLNTVRALL
AFRRSHPALFDGDLSLVDVGDDLLGFTRQKGDETLLCVFNLTGQEQQTTL
PVEVASDLPVAHFTATRDGSTLTLPAYQAAFMQVA
3D structure
PDB3wy2 Structural analysis of the alpha-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism
ChainA
Resolution1.471 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 E271 H332 D333
Catalytic site (residue number reindexed from 1) D97 R197 D199 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 D23 R25 V29 D31 D20 R22 V26 D28
BS02 GOL A S104 D172 V173 F206 Y207 H209 D243 S101 D169 V170 F203 Y204 H206 D240
BS03 GOL A P178 R181 Q182 P175 R178 Q179
BS04 GOL A P247 E283 P244 E280
BS05 BGC A D62 Y65 H105 R200 D202 E271 H332 D333 R400 D59 Y62 H102 R197 D199 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
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Biological Process
External links
PDB RCSB:3wy2, PDBe:3wy2, PDBj:3wy2
PDBsum3wy2
PubMed26057678
UniProtH3K096

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