Structure of PDB 2bhy Chain A

Receptor sequence
>2bhyA (length=580) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
SFQTQHDPRTRLGATPLPGGAGTRFRLWTSTARTVAVRVNGTEHVMTSLG
GGIYELELPVGPGARYLFVLDGVPTPDPYARFLPDGVHGEAEVVDFGTFD
WTDADWHGIKLADCVFYEVHVGTFTPEGTYRAAAEKLPYLKELGVTAIQV
MPLAAFDGQRGWGYDGAAFYAPYAPYGRPEDLMALVDAAHRLGLGVFLDV
VYNHFGPSGNYLSSYAPSYFTDRFSSAWGMGLDYAEPHMRRYVTGNARMW
LRDYHFDGLRLDATPYMTDDSETHILTELAQEIHELGGTHLLLAEDHRNL
PDLVTVNHLDGIWTDDFHHETRVTLTGEQEGYYAGYRGGAEALAYTIRRG
WRYEGQFWAVKGEEHERGHPSDALEAPNFVYCIQNHDQIGNRPLGERLHQ
SDGVTLHEYRGAAALLLTLPMTPLLFQGQEWAASTPFQFFSDHAGELGQA
VSEGRKKEFDVPDPQAEQTFLNSKLNWAEREGGEHARTLRLYRDLLRLRR
EDPVLHNRQRENLTTGHDGDVLWVRTVTGAGERVLLWNLGQDTRAVAEVK
LPFTVPRRLLLHTEGREDLTLGAGEAVLVG
3D structure
PDB2bhy Crystal Structure of Maltooligosyltrehalose Trehalohydrolase from Deinococcus Radiodurans in Complex with Disaccharides
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L156 G157 T159 G179
Catalytic site (residue number reindexed from 1) L143 G144 T146 G166
Enzyme Commision number 3.2.1.141: 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005992 trehalose biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2bhy, PDBe:2bhy, PDBj:2bhy
PDBsum2bhy
PubMed15784255
UniProtQ9RX51|TREZ_DEIRA Malto-oligosyltrehalose trehalohydrolase (Gene Name=treZ)

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