Structure of PDB 2y0c Chain B

Receptor sequence
>2y0cB (length=450) Species: 292 (Burkholderia cepacia) [Search protein sequence]
GSMNLTIIGSGSVGLVTGACLADIGHDVFCLDVDQAKIDILNNGGVPIHE
PGLKEVIARNRSAGRLRFSTDIEAAVAHGDVQFIAVGTPDLQYVLAAARN
IGRYMTGFKVIVDKSTVPVGTAERVRAAVAEELAKRQMFSVVSNPEFLKE
GAAVDDFTRPDRIVIGCDDDVPGERARELMKKLYAPFNRNHERTLYMDVR
SAEFTKYAANAMLATRISFMNELANLADRFGADIEAVRRGIGSDPRIGYH
FLYAGCGYGGSCFPKDVEALIRTADEHGQSLQILKAVSSVNATQKRVLAD
KIVARFGEDLTGRTFAIWGLAFKPNTDDMREAPSRELIAELLSRGARIAA
YDPVAQEEARRVIALDLADHPSWLERLSFVDDEAQAARDADALVIVTEWK
IFKSPDFVALGRLWKTPVIFDGRNLYEPETMSEQGIEYHPIGRPGSRQAV
3D structure
PDB2y0c Structure of Burkholderia Cepacia Udp-Glucose Dehydrogenase (Ugd) Bcec and Role of Tyr10 in Final Hydrolysis of Ugd Thioester Intermediate.
ChainB
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T121 E158 K214 N218 C270 D274
Catalytic site (residue number reindexed from 1) T116 E150 K206 N210 C262 D266
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 K214 I225 F259 Y261 Y266 C270 F271 F330 K331 E146 F147 L148 K206 I217 F251 Y253 Y258 C262 F263 F322 K323
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2y0c, PDBe:2y0c, PDBj:2y0c
PDBsum2y0c
PubMed21602353
UniProtC9E261

[Back to BioLiP]