Structure of PDB 2by2 Chain A

Receptor sequence
>2by2A (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
PDB2by2 Is Radiation Damage Dependent on the Dose-Rate Used During Macromolecular Crystallography Data Collection?
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
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 T337 G340 R350 G351 T324 G327 R337 G338
BS02 GLC A H310 E376 H297 E363
BS03 GLC A E249 H251 E236 H238
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:2by2, PDBe:2by2, PDBj:2by2
PDBsum2by2
PubMed16421442
UniProtQ9RX51|TREZ_DEIRA Malto-oligosyltrehalose trehalohydrolase (Gene Name=treZ)

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