Structure of PDB 3wy1 Chain B

Receptor sequence
>3wy1B (length=535) Species: 1076127 (Halomonas sp. H11) [Search protein sequence]
NMMWWRGGVIYQIYPRSFLDSRGDGVGDLNGITEKLDYVASLNVDGIWLS
PFFTSPMLDFGYDVSDYRDVDPMFGTLEDFKALLEKAHSLGLKVMIDQVI
SHTSDQHPWFQESRQNRTNPKADWFVWADPKPDGTPPNNWLSIFGGSAWT
FDSRRQQYYLHNFLTSQPDVNFHHPEARQAQLDNMRFWLDLGVDGFRLDT
VNFYFHDAELRDNPPVPKGEAKTLGAPEANPYTWQRHVYDLSRPENLDFL
KDLRALMDEYPGTTTVGEIGDDNPLERMAEYTAGGDKLHMAYTFDLLNMP
HSASYLREVIERFQRLAGDAWPCWATSNHDVVRSATRWGADEDPHAYPKV
MLAVLFSLRGSVCLYQGEELGLPEADVPFERIQDPYGKVLWPEFKGRDGC
RTPMPWTDGEQGGFSPVEPWLPMEARHLELAVSRQQDDPNATLNTVRALL
AFRRSHPALFDGDLSLVDVGDDLLGFTRQKGDETLLCVFNLTGQEQQTTL
PVEVASDLPVAHFTATRDGSTLTLPAYQAAFMQVA
3D structure
PDB3wy1 Structural analysis of the alpha-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism
ChainB
Resolution2.15 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 B D23 D27 V29 D31 D20 D24 V26 D28
BS02 PRU B D62 Y65 H105 F147 F166 R200 D202 T203 G228 E271 F297 H332 D333 R400 D59 Y62 H102 F144 F163 R197 D199 T200 G225 E268 F294 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:3wy1, PDBe:3wy1, PDBj:3wy1
PDBsum3wy1
PubMed26057678
UniProtH3K096

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