Structure of PDB 3mkk Chain B

Receptor sequence
>3mkkB (length=664) Species: 411459 (Blautia obeum ATCC 29174) [Search protein sequence]
AMIRKYRYGAPFDTEALTEKIETAEEAFPYGEISQKEGFAFTYIMDEDDI
VYGLGESNRGINKRGYCYISNCTDDPIHTEDKRSLYGAHNFIIVSGKTTF
GLFFDYPSKLTFDIGYTRMDTLKVSCENADLDIYVIEGENAYDIVKQFRR
VIGRSYIPPKFAFGFGQSRWGYTTKEDFRAVAKGYRENHIPIDMIYMDID
YMQDFKDFTVNEKNFPDFPEFVKEMKDQELRLIPIIDAGVKVEKGYEVYE
EGVKNNYFCKREDGSDFVAAVWPGDTHFPDMLNPEARKWFGDKYRFLIDQ
GIEGFWNAMNEPAIFYSSEGLAEAKEFAGEFAKDTEGKIHPWAMQAKMKD
IVNSPEDYKRFYHNVNGKKIRHDKVHNLFGYNMTRAAGEAFERIDPEKRF
LMFSRSSYIGMHRYGGIWMGDNKSWWSHILLNLKMLPSLNMCGFMYTGAD
LGGFGDDTTRDLLLRFLALGVFTPLMRDHAAEGTREQECYQFENIEDFRS
VINARYRLVPYLYSEYMKAALNDDMYFKPLGFVYPDDKMAIRVEDQLMLG
NEIMIAPVYEQNARGRYVYLPEEMKFIKFMPDGSISEEVLEKGVHYVDVA
LNEVPLFIRSGKCIPVAEAAECVKDIDTENMQLIGYEGSSYTLYEDDGIH
KDYDKKENYRVLTK
3D structure
PDB3mkk The Crystal Structures Of The Glycoside Hydrolase (Family 31) From Ruminococcus Obeum Atcc 29174
ChainB
Resolution1.91 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 BGC B D73 P75 W169 W271 R404 D420 D74 P76 W170 W272 R405 D421
BS02 GLC B W169 D197 I198 R404 W417 D420 F453 H478 W170 D198 I199 R405 W418 D421 F454 H479
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:3mkk, PDBe:3mkk, PDBj:3mkk
PDBsum3mkk
PubMed20581222
UniProtA5ZY13

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