Structure of PDB 5v0t Chain E

Receptor sequence

>5v0tE (length=457) Species: 266265 (Paraburkholderia xenovorans LB400)

GRLIIVSNRVAPISEGGPAAGGLAVGVYDALKETGGMWFGWSGDVLSSGQ
PQIKVEERGPVTFATIALMRRDYDQYYRGFSNATLWPAFHYRADLLQYDR
HDFEGYWRVNAWLAQQLVPLLREDDVIWVHDYHLIPFAQALRAAGVKNRI
GFFLHIPFPASQVLLAVPPHRELVEALCSFDLLGFQTAPDLRAFCDYIVN
EANGTADPSASGPLTIHAFGRTLRAAAYPIGVYPDEIAELAKAGERGKPV
RTMKATLHSRKLIMSVDRLDYSKGLVERFRAFERLLEHSTAQRNKVSFLQ
IAPPTRADMHAYQDIRLQLEGESGRINGRFAELDWTPILYIHKQYERSVL
AALFRTAHVGYVTPLRDGMNLVAKEYVSAQDPENPGVLVLSRFAGAAQEL
DGALIVNPVDIDGMAEALARALDMPLAERQARHRDMMVQLRENNVSVWRD
NFMRDLQ

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: E
• Resolution: 1.95 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H164 D376
• Catalytic site (residue number reindexed from 1): H155 D367
• 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	E	A29 G30 G31 V34 V275 R277 K282 Q353 Y354 L359 N379 L380 V381 E384	A20 G21 G22 V25 V266 R268 K273 Q344 Y345 L350 N370 L371 V372 E375
BS02	G6P	E	R18 L32 Y86 D140 R315	R9 L23 Y77 D131 R306
BS03	OXD	E	R364 T365 A366 N393 G395	R355 T356 A357 N384 G386

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