Structure of PDB 2y0d Chain D

Receptor sequence
>2y0dD (length=453) Species: 292 (Burkholderia cepacia) [Search protein sequence]
SMNLTIIGSGKVGLVTGACLADIGHDVFCLDVDQAKIDILNNGGVPIHEP
GLKEVIARNRSAGRLRFSTDIEAAVAHGDVQFIAVGTPPGSADLQYVLAA
ARNIGRYMTGFKVIVDKSTVPVGTAERVRAAVAEELAKRGGDQMFSVVSN
PEFLKEGAAVDDFTRPDRIVIGCDDDVPGERARELMKKLYAPFNRNHERT
LYMDVRSAEFTKYAANAMLATRISFMNELANLADRFGADIEAVRRGIGSD
PRIGYHFLYAGCGYGGSCFPKDVEALIRTADEHGQSLQILKAVSSVNATQ
KRVLADKIVARFGEDLTGRTFAIWGLAFKPNTDDMREAPSRELIAELLSR
GARIAAYDPVAQEEARRVIALDLADHPSWLERLSFVDDEAQAARDADALV
IVTEWKIFKSPDFVALGRLWKTPVIFDGRNLYEPETMSEQGIEYHPIGRP
GSR
3D structure
PDB2y0d Structure of Burkholderia Cepacia Udp-Glucose Dehydrogenase (Ugd) Bcec and Role of Tyr10 in Final Hydrolysis of Ugd Thioester Intermediate.
ChainD
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T121 E158 K214 N218 C270 D274
Catalytic site (residue number reindexed from 1) T119 E156 K212 N216 C268 D272
Enzyme Commision number 1.1.1.22: UDP-glucose 6-dehydrogenase.
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 UGA D E154 F155 L156 E158 K214 I225 F259 Y261 Y266 C270 F271 F330 K331 E152 F153 L154 E156 K212 I223 F257 Y259 Y264 C268 F269 F328 K329
Gene Ontology
Molecular Function
GO:0003979 UDP-glucose 6-dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding
Biological Process
GO:0000271 polysaccharide biosynthetic process
GO:0006065 UDP-glucuronate biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2y0d, PDBe:2y0d, PDBj:2y0d
PDBsum2y0d
PubMed21602353
UniProtC9E261

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