Structure of PDB 5zcc Chain A

Receptor sequence
>5zccA (length=545) Species: 1409 (Bacillus sp. (in: firmicutes)) [Search protein sequence]
KWWKEAVAYQIYPRSFMDSNGDGIGDIQGVISKLDYLSDLGIDVIWICPI
YQSPNDDNGYDISDYKDIMKDFGTMEDFDELLDEVHHRGMKLIMDLVINH
TSDEHPWFLESRSAKENPYRDYYIWHEGKDGKEPNNWESIFSGSAWEFDE
KTKEYYMHVFSKKQPDLNWENEKVRHELYEMVNWWLDKGIDGFRVDAISH
IKKVAGFPDLPNPEKLDYVPSFEGHMNRPGIQEHLKELKEKTFAKYDIMT
VGQANGVTSDSADEWVAEDGGNFNMIFQFEHMGLWKPLDLIELKTILTNW
QNGLEKINGWNALYLENHDQIRSVNKFGSTAYRVESAKCLAALYFLMKGT
PFIYQGQELGMTNVKFDSIDDYDDVGMINYYRIQREKGDSHDEIMKVIWE
TGRDNSRTPMQWNTEKNAGFSTGNPWMKVNPNYVDINVEEQKSDKNSVLN
FYKQLIKIRKQHDVLVYGTYKLLAEEDSAIYAYTRTLEGKTAVVICNMSP
NNQTFEFPSSFTNIEVLIHNYPLDKNETLEQCTLHPYETRVYLIS
3D structure
PDB5zcc Function and structure of GH13_31 alpha-glucosidase with high alpha-(1→4)-glucosidic linkage specificity and transglucosylation activity.
ChainA
Resolution1.704 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D98 R197 D199 Q256 H326 D327
Catalytic site (residue number reindexed from 1) D95 R194 D196 Q253 H318 D319
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 I143 A200 H203 Q256 N258 I140 A197 H200 Q253 N255
BS02 GLC A D60 Y63 H103 F163 D199 Q256 H326 D327 R411 D57 Y60 H100 F160 D196 Q253 H318 D319 R403
BS03 CA A D21 N23 D25 I27 D29 D18 N20 D22 I24 D26
BS04 CA A D534 E537 T543 D524 E527 T533
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5zcc, PDBe:5zcc, PDBj:5zcc
PDBsum5zcc
PubMed29870070
UniProtA0A2Z5WH92

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