Structure of PDB 8ids Chain A

Receptor sequence
>8idsA (length=543) Species: 1409 (Bacillus sp. (in: firmicutes)) [Search protein sequence]
EKKWWKEAVAYQIYPRSFMDSNGDGIGDIQGVISKLDYLSDLGIDVIWIC
PIYQSPNDDNGYDISDYKDIMKDFGTMEDFDELLDEVHHRGMKLIMDLVI
NHTSDEHPWFLESRSAKENPYRDYYIWHEGKDGKEPNNWESIFSGSAWEF
DEKTKEYYMHVFSKKQPDLNWENEKVRHELYEMVNWWLDKGIDGFRVDAI
SHIKKVAGFPDLPNPEKLDYVPSFEGHMNRPGIQEHLKELKEKTFAKYDI
MTVGQAPGVTSDSADEWVAEDGGNFNMIFQFEHMGPLDLIELKTILTNWQ
NGLEKINGWNALYLENHDQIRSVNKFGSTAYRVESAKCLAALYFLMKGTP
FIYQGQELGMTNVKFDSIDDYDDVGMINYYRIQREKGDSHDEIMKVIWET
GRDNSRTPMQWNTEKNAGFSTGNPWMKVNPNYVDINVEEQKSDKNSVLNF
YKQLIKIRKQHDVLVYGTYKLLAEEDSAIYAYTRTLEGKTAVVICNMSPN
NQTFEFPFTNIEVLIHNYPLDKNETLEQCTLHPYETRVYLLSL
3D structure
PDB8ids Alteration of Substrate Specificity and Transglucosylation Activity of GH13_31 alpha-Glucosidase from Bacillus sp. AHU2216 through Site-Directed Mutagenesis of Asn258 on beta → alpha Loop 5.
ChainA
Resolution1.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 GLC A F163 A200 H203 Q256 F162 A199 H202 Q255
BS02 GLC A D60 Y63 H103 F163 R197 D199 Q256 H326 D327 R411 D59 Y62 H102 F162 R196 D198 Q255 H317 D318 R402
BS03 CA A D21 N23 D25 I27 D29 D20 N22 D24 I26 D28
BS04 CA A E537 T543 E524 T530
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0016787 hydrolase activity
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:8ids, PDBe:8ids, PDBj:8ids
PDBsum8ids
PubMed37049872
UniProtA0A2Z5WH92

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