Structure of PDB 2y0d Chain B

Receptor sequence
>2y0dB (length=448) Species: 292 (Burkholderia cepacia) [Search protein sequence]
SMNLTIIGSGKVGLVTGACLADIGHDVFCLDVDQAKIDILNNGGVPIHEP
GLKEVIARNRSAGRLRFSTDIEAAVAHGDVQFIAVGTPSADLQYVLAAAR
NIGRYMTGFKVIVDKSTVPVGTAERVRAAVAEELAKRGGQMFSVVSNPEF
LKEGAAVDDFTRPDRIVIGCDDDVPGERARELMKKLYAPFNRNHERTLYM
DVRSAEFTKYAANAMLATRISFMNELANLADRFGADIEAVRRGIGSDPRI
GYHFLYAGCGYGGSCFPKDVEALIRTADEHGQSLQILKAVSSVNATQKRV
LADKIVARFGEDLTGRTFAIWGLAFKPNTDDMREAPSRELIAELLSRGAR
IAAYDPVAQEEARRVIALDLADHPSWLERLSFVDDEAQAARDADALVIVT
EWKIFKSPDFVALGRLWKTPVIFDGRNLYEPETMSEQGIEYHPIGRPG
3D structure
PDB2y0d Structure of Burkholderia Cepacia Udp-Glucose Dehydrogenase (Ugd) Bcec and Role of Tyr10 in Final Hydrolysis of Ugd Thioester Intermediate.
ChainB
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) T117 E153 K209 N213 C265 D269
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 B E154 F155 L156 E158 K214 I225 F259 Y261 Y266 C270 F271 F330 K331 E149 F150 L151 E153 K209 I220 F254 Y256 Y261 C265 F266 F325 K326
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
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Biological Process
External links
PDB RCSB:2y0d, PDBe:2y0d, PDBj:2y0d
PDBsum2y0d
PubMed21602353
UniProtC9E261

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