Structure of PDB 1uqu Chain A

Receptor sequence
>1uquA (length=452) Species: 562 (Escherichia coli) [Search protein sequence]
SRLVVVSNRIAPPDSAGGLAVGILGALKAAGGLWFGWSGETGNEDQPLKK
VKKGNITWASFNLSEQDLDEYYNQFSNAVLWPAFHYRLDLVQFQRPAWDG
YLRVNALLADKLLPLLQDDDIIWIHDYHLLPFAHELRKRGVNNRIGFFLH
IPFPTPEIFNALPTYDTLLEQLCDYDLLGFQTENDRLAFLDCLSNLTRVT
TRSAKSHTAWGKAFRTEVYPIGIEPKEIAKQAAGPLPPKLAQLKAELKNV
QNIFSVERLDYSKGLPERFLAYEALLEKYPQHHGKIRYTQIAPTSRGDVQ
AYQDIRHQLENEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFRYSDVG
LVTPLRDGMNLVAKEYVAAQDPANPGVLVLSQFAGAANELTSALIVNPYD
RDEVAAALDRALTMSLAERISRHAEMLDVIVKNDINHWQECFISDLKQIV
PR
3D structure
PDB1uqu The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H154 D361
Catalytic site (residue number reindexed from 1) H150 D357
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 UPG A H154 R262 K267 H338 F339 R341 L344 D361 G362 M363 N364 L365 V366 E369 H150 R258 K263 H334 F335 R337 L340 D357 G358 M359 N360 L361 V362 E365
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
GO:0006950 response to stress
GO:0006970 response to osmotic stress
GO:0006974 DNA damage response
GO:0070415 trehalose metabolism in response to cold stress

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Molecular Function
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Biological Process
External links
PDB RCSB:1uqu, PDBe:1uqu, PDBj:1uqu
PDBsum1uqu
PubMed14570926
UniProtP31677|OTSA_ECOLI Trehalose-6-phosphate synthase (Gene Name=otsA)

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