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1UQU

Trehalose-6-phosphate from E. coli bound with UDP-glucose.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003825molecular_functionalpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
A0005992biological_processtrehalose biosynthetic process
A0006950biological_processresponse to stress
A0006970biological_processresponse to osmotic stress
A0006974biological_processDNA damage response
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016758molecular_functionhexosyltransferase activity
B0003824molecular_functioncatalytic activity
B0003825molecular_functionalpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
B0005992biological_processtrehalose biosynthetic process
B0006950biological_processresponse to stress
B0006970biological_processresponse to osmotic stress
B0006974biological_processDNA damage response
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016758molecular_functionhexosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE UPG A1457
ChainResidue
ATRP85
APHE339
AARG341
ALEU344
AASP361
AGLY362
AMET363
AASN364
ALEU365
AVAL366
AGLU369
AHIS154
AHOH2052
AHOH2069
AHOH2070
AHOH2072
AHOH2073
AGLN185
AILE225
AVAL260
AARG262
ALYS267
APRO297
AHIS338

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14570926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14570926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UQT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UQU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Involved in alpha anomer selectivity","evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uqt
ChainResidueDetails
AASP361
AHIS154

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uqt
ChainResidueDetails
BASP361
BHIS154

site_idMCSA1
Number of Residues2
DetailsM-CSA 622
ChainResidueDetails
AHIS154electrostatic stabiliser
AASP361electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 622
ChainResidueDetails
BHIS154electrostatic stabiliser
BASP361electrostatic stabiliser

238582

PDB entries from 2025-07-09

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