Structure of PDB 6jbr Chain D

Receptor sequence
>6jbrD (length=465) Species: 242507 (Pyricularia oryzae 70-15) [Search protein sequence]
RLLLISNRLPITIKRSDDGQYSFSMSSGGLVTGLSGLAKTTSFQWYGWPG
LEVPDAEAGPVVQRLKNEYGAHPVFVDDELADRHYNGFANSILWPLFHYH
PGEITFDESAWSAYKEVNRLFAQTVVKDVQDGDMIWVHDYHLMLLPEMLR
EEIGDSKKNVKIGFFLHTPFPSSEIYRILPVRQALLQGVLHCDLLGFHTY
DYARHFLSSCSRILSAPTTPNGVQFAGRFVTVGAFPIGIDPEKFVEGLQK
PKVQQRIAALTRKFEGVKLIVGVDRLDYIKGVPQKLHALEVFLTEHPEWI
GKIVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGKFGTIEFMPIHFLHQ
SVSFDELAALYAVSDVCLVSSTRDGMNLVSYEYIATQRDRHGVMILSEFT
GAAQSLSGSLIVNPWNTEELANAIHDAVTMGPEQREANFKKLERYVFKYT
SAWWGSSFVAELNRL
3D structure
PDB6jbr Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1.
ChainD
Resolution2.03 Å
3D
structure
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Enzymatic activity
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 GLC D G43 H181 H212 D388 G389 M390 G29 H167 H198 D374 G375 M376
BS02 G6P D R22 L44 Y99 D153 R289 R327 R8 L30 Y85 D139 R275 R313
BS03 UDP D S41 G42 G43 T46 R289 K294 V324 S365 N391 L392 V393 E396 S27 G28 G29 T32 R275 K280 V310 S351 N377 L378 V379 E382
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003825 alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
Biological Process
GO:0005992 trehalose biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6jbr, PDBe:6jbr, PDBj:6jbr
PDBsum6jbr
PubMed31455720
UniProtG4NHF4

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