Structure of PDB 1gz5 Chain C

Receptor sequence
>1gz5C (length=456) Species: 316407 (Escherichia coli str. K-12 substr. W3110) [Search protein sequence]
SRLVVVSNRIAPPDEHAASAGGLAVGILGALKAAGGLWFGWSGETGNEDQ
PLKKVKKGNITWASFNLSEQDLDEYYNQFSNAVLWPAFHYRLDLVQFQRP
AWDGYLRVNALLADKLLPLLQDDDIIWIHDYHLLPFAHELRKRGVNNRIG
FFLHIPFPTPEIFNALPTYDTLLEQLCDYDLLGFQTENDRLAFLDCLSNL
TRVTTRSAKSHTAWGKAFRTEVYPIGIEPKEIAKQAAGPLPPKLAQLKAE
LKNVQNIFSVERLDYSKGLPERFLAYEALLEKYPQHHGKIRYTQIAPTSR
GDVQAYQDIRHQLENEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFRY
SDVGLVTPLRDGMNLVAKEYVAAQDPANPGVLVLSQFAGAANELTSALIV
NPYDRDEVAAALDRALTMSLAERISRHAEMLDVIVKNDINHWQECFISDL
KQIVPR
3D structure
PDB1gz5 Insights Into Trehalose Synthesis Provided by the Structure of the Retaining Glycosyltransferase Otsa
ChainC
Resolution2.43 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) H154 D361
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 UDP C G21 G22 R262 H338 F339 L344 L365 V366 E369 G21 G22 R262 H338 F339 L344 L365 V366 E369
BS02 G6P C R9 L23 Y76 D130 R300 R9 L23 Y76 D130 R300
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:1gz5, PDBe:1gz5, PDBj:1gz5
PDBsum1gz5
PubMed12498887
UniProtP31677|OTSA_ECOLI Trehalose-6-phosphate synthase (Gene Name=otsA)

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