Structure of PDB 2y0c Chain D

Receptor sequence
>2y0cD (length=454) Species: 292 (Burkholderia cepacia) [Search protein sequence]
GSMNLTIIGSGSVGLVTGACLADIGHDVFCLDVDQAKIDILNNGGVPIHE
PGLKEVIARNRSAGRLRFSTDIEAAVAHGDVQFIAVGTPPDLQYVLAAAR
NIGRYMTGFKVIVDKSTVPVGTAERVRAAVAEELAKRGGDQMFSVVSNPE
FLKEGAAVDDFTRPDRIVIGCDDDVPGERARELMKKLYAPFNRNHERTLY
MDVRSAEFTKYAANAMLATRISFMNELANLADRFGADIEAVRRGIGSDPR
IGYHFLYAGCGYGGSCFPKDVEALIRTADEHGQSLQILKAVSSVNATQKR
VLADKIVARFGEDLTGRTFAIWGLAFKPNTDDMREAPSRELIAELLSRGA
RIAAYDPVAQEEARRVIALDLADHPSWLERLSFVDDEAQAARDADALVIV
TEWKIFKSPDFVALGRLWKTPVIFDGRNLYEPETMSEQGIEYHPIGRPGS
RQAV
3D structure
PDB2y0c Structure of Burkholderia Cepacia Udp-Glucose Dehydrogenase (Ugd) Bcec and Role of Tyr10 in Final Hydrolysis of Ugd Thioester Intermediate.
ChainD
Resolution1.75 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 E154 K210 N214 C266 D270
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 E150 F151 L152 E154 K210 I221 F255 Y257 Y262 C266 F267 F326 K327
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:2y0c, PDBe:2y0c, PDBj:2y0c
PDBsum2y0c
PubMed21602353
UniProtC9E261

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