Structure of PDB 2bxy Chain A

Receptor sequence

>2bxyA (length=580) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539)

SFQTQHDPRTRLGATPLPGGAGTRFRLWTSTARTVAVRVNGTEHVMTSLG
GGIYELELPVGPGARYLFVLDGVPTPDPYARFLPDGVHGEAEVVDFGTFD
WTDADWHGIKLADCVFYEVHVGTFTPEGTYRAAAEKLPYLKELGVTAIQV
MPLAAFDGQRGWGYDGAAFYAPYAPYGRPEDLMALVDAAHRLGLGVFLDV
VYNHFGPSGNYLSSYAPSYFTDRFSSAWGMGLDYAEPHMRRYVTGNARMW
LRDYHFDGLRLDATPYMTDDSETHILTELAQEIHELGGTHLLLAEDHRNL
PDLVTVNHLDGIWTDDFHHETRVTLTGEQEGYYAGYRGGAEALAYTIRRG
WRYEGQFWAVKGEEHERGHPSDALEAPNFVYCIQNHDQIGNRPLGERLHQ
SDGVTLHEYRGAAALLLTLPMTPLLFQGQEWAASTPFQFFSDHAGELGQA
VSEGRKKEFDVPDPQAEQTFLNSKLNWAEREGGEHARTLRLYRDLLRLRR
EDPVLHNRQRENLTTGHDGDVLWVRTVTGAGERVLLWNLGQDTRAVAEVK
LPFTVPRRLLLHTEGREDLTLGAGEAVLVG

3D structure

• PDB: 2bxy Is Radiation Damage Dependent on the Dose-Rate Used During Macromolecular Crystallography Data Collection?
• Chain: A
• Resolution: 1.75 Å

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	P314 D315 P383	P301 D302 P370
BS03	GLC	A	H310 E376	H297 E363
BS04	GLC	A	W41 E249 H251	W28 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

External links

• PDB: RCSB:2bxy, PDBe:2bxy, PDBj:2bxy
• PDBsum: 2bxy
• PubMed: 16421442
• UniProt: Q9RX51|TREZ_DEIRA Malto-oligosyltrehalose trehalohydrolase (Gene Name=treZ)