Structure of PDB 5v0t Chain A

Receptor sequence

>5v0tA (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: A
• 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	A	A29 G30 G31 V34 V275 R277 K282 P312 Q353 Y354 R356 L359 N379 L380 V381 E384	A16 G17 G18 V21 V262 R264 K269 P299 Q340 Y341 R343 L346 N366 L367 V368 E371
BS02	G6P	A	R18 L32 Y86 D140 R315	R9 L19 Y73 D127 R302
BS03	OXD	A	K352 Y354	K339 Y341

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