Structure of PDB 5v0t Chain G

Receptor sequence

>5v0tG (length=454) Species: 266265 (Paraburkholderia xenovorans LB400)

GRLIIVSNRVAPIPAAGGLAVGVYDALKETGGMWFGWSGDVLSSGQPQIK
VEERGPVTFATIALMRRDYDQYYRGFSNATLWPAFHYRADLLQYDRHDFE
GYWRVNAWLAQQLVPLLREDDVIWVHDYHLIPFAQALRAAGVKNRIGFFL
HIPFPASQVLLAVPPHRELVEALCSFDLLGFQTAPDLRAFCDYIVNEANG
TADPSASGPLTIHAFGRTLRAAAYPIGVYPDEIAELAKAGERGKPVRTMK
ATLHSRKLIMSVDRLDYSKGLVERFRAFERLLEHSTAQRNKVSFLQIAPP
TRADMHAYQDIRLQLEGESGRINGRFAELDWTPILYIHKQYERSVLAALF
RTAHVGYVTPLRDGMNLVAKEYVSAQDPENPGVLVLSRFAGAAQELDGAL
IVNPVDIDGMAEALARALDMPLAERQARHRDMMVQLRENNVSVWRDNFMR
DLQG

3D structure

• PDB: 5v0t Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate
• Chain: G
• Resolution: 1.95 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H164 D376
• Catalytic site (residue number reindexed from 1): H151 D363
• 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	G	A29 G30 G31 V275 R277 K282 Q353 Y354 R356 L359 N379 L380 V381 E384	A16 G17 G18 V262 R264 K269 Q340 Y341 R343 L346 N366 L367 V368 E371
BS02	G6P	G	R18 L32 Y86 D140 R315	R9 L19 Y73 D127 R302

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• 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

External links

• PDB: RCSB:5v0t, PDBe:5v0t, PDBj:5v0t
• PDBsum: 5v0t
• UniProt: Q13W28