Structure of PDB 5uof Chain B

Receptor sequence
>5uofB (length=459) Species: 395019 (Burkholderia multivorans ATCC 17616) [Search protein sequence]
MSRLIVVSNRVAIGEDTRPSAGGLAVGVMDALQETGGVWFGWNGEIVGTP
DAAPAIRRDGNVTYATVGLTRRDYDQYYRGFSNATLWPVFHYRGDLARFD
RQEYAGYLRVNAMLAKQLAALLRPDDLIWVHDYHLLPFAHALRELGVKNP
IGFFLHIPFPSPDVLRLVPPHDELVKFMCAYDVTGFQTDADRQAFTDYIE
RRGIGTASEDGMLHAHGRVVKVAAYPIGVYPDAIAQAAVQYGARKPVKML
RDALGGRKLVMSVDRLDYSKGLVERFQAFERMLANAPGWQGRVSLVQIAP
PTDVQTYQRIRETLEGEAGRINGRFSQLDWTPIQYLNRKYERNLLMAFFR
MSQVGYVTPLRDGMNLVAKEYVASQDPADPGVLVLSEFAGAAAELTGALL
VNPYDLSQMADALERALSMPLAERQARHEENLARLRANDLSVWRDTFVAD
LRSVAAAAS
3D structure
PDB5uof Crystal structure of alpha,alpha-trehalose 6-phosphate sythase from Burkholderia multivorans
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H164 D372
Catalytic site (residue number reindexed from 1) H156 D362
Enzyme Commision number 2.4.1.15: alpha,alpha-trehalose-phosphate synthase (UDP-forming).
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 SER B F107 P177 P178 F99 P169 P170
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003825 alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005992 trehalose biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5uof, PDBe:5uof, PDBj:5uof
PDBsum5uof
PubMed
UniProtA0A0H3KGN3

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