Structure of PDB 6c9z Chain B

Receptor sequence
>6c9zB (length=663) Species: 411459 (Blautia obeum ATCC 29174) [Search protein sequence]
MIRKYRYGAPFDTEALTEKIETAEEAFPYGEISQKEGFAFTYIMDEDDIV
YGLGESNRGINKRGYCYISNCTDDPIHTEDKRSLYGAHNFIIVSGKTTFG
LFFDYPSKLTFDIGYTRMDTLKVSCENADLDIYVIEGENAYDIVKQFRRV
IGRSYIPPKFAFGFGQSRYGYTTKEDFRAVAKGYRENHIPIDMIYMDIDY
MQDFKDFTVNEKNFPDFPEFVKEMKDQELRLIPIIDAGVKVEKGYEVYEE
GVKNNYFCKREDGSDFVAAVWPGDTHFPDMLNPEARKWFGDKYRFLIDQG
IEGFWNDMNEPAIFYSSEGLAEAKEFAGEFAKDTEGKIHPWAMQAKMKDI
VNSPEDYKRFYHNVNGKKIRHDKVHNLFGYNMTRAAGEAFERIDPEKRFL
MFSRSSYIGMHRYGGIWMGDNKSWWSHILLNLKMLPSLNMCGFMYTGADL
GGFGDDTTRDLLLRFLALGVFTPLMRDHAAEGTREQECYQFENIEDFRSV
INARYRLVPYLYSEYMKAALNDDMYFKPLGFVYPDDKMAIRVEDQLMLGN
EIMIAPVYEQNARGRYVYLPEEMKFIKFMPDGSISEEVLEKGVHYVDVAL
NEVPLFIRSGKCIPVAEAAECVKDIDTENMQLIGYEGSSYTLYEDDGIHK
DYDKKENYRVLTK
3D structure
PDB6c9z THE CRYSTAL STRUCTURE OF THE alpha-Glucosidase (GH 31) W169Y mutant FROM RUMINOCOCCUS OBEUM ATCC 29174 in complex with voglibose
ChainB
Resolution2.101 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 VOG B D73 Y169 D197 I198 W271 D307 M308 R404 D420 F453 H478 D73 Y169 D197 I198 W271 D307 M308 R404 D420 F453 H478
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
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Biological Process
External links
PDB RCSB:6c9z, PDBe:6c9z, PDBj:6c9z
PDBsum6c9z
PubMed
UniProtA5ZY13

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