Structure of PDB 3pha Chain D

Receptor sequence
>3phaD (length=666) Species: 411459 (Blautia obeum ATCC 29174) [Search protein sequence]
SNAMIRKYRYGAPFDTEALTEKIETAEEAFPYGEISQKEGFAFTYIMDED
DIVYGLGESNRGINKRGYCYISNCTDDPIHTEDKRSLYGAHNFIIVSGKT
TFGLFFDYPSKLTFDIGYTRMDTLKVSCENADLDIYVIEGENAYDIVKQF
RRVIGRSYIPPKFAFGFGQSRYGYTTKEDFRAVAKGYRENHIPIDMIYMD
IDYMQDFKDFTVNEKNFPDFPEFVKEMKDQELRLIPIIDAGVKVEKGYEV
YEEGVKNNYFCKREDGSDFVAAVWPGDTHFPDMLNPEARKWFGDKYRFLI
DQGIEGFWNDMNEPAIFYSSEGLAEAKEFAGEFAKDTEGKIHPWAMQAKM
KDIVNSPEDYKRFYHNVNGKKIRHDKVHNLFGYNMTRAAGEAFERIDPEK
RFLMFSRSSYIGMHRYGGIWMGDNKSWWSHILLNLKMLPSLNMCGFMYTG
ADLGGFGDDTTRDLLLRFLALGVFTPLMRDHAAEGTREQECYQFENIEDF
RSVINARYRLVPYLYSEYMKAALNDDMYFKPLGFVYPDDKMAIRVEDQLM
LGNEIMIAPVYEQNARGRYVYLPEEMKFIKFMPDGSISEEVLEKGVHYVD
VALNEVPLFIRSGKCIPVAEAAECVKDIDTENMQLIGYEGSSYTLYEDDG
IHKDYDKKENYRVLTK
3D structure
PDB3pha The crystal structure of the W169Y mutant of alpha-glucosidase (gh31 family) from Ruminococcus obeum atcc 29174 in complex with acarbose
ChainD
Resolution2.173 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.-
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 D I76 K422 I79 K425
BS02 AC1 D D73 Y169 D197 I198 W271 D307 M308 R404 D420 H478 D76 Y172 D200 I201 W274 D310 M311 R407 D423 H481
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3pha, PDBe:3pha, PDBj:3pha
PDBsum3pha
PubMed
UniProtA5ZY13

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