Structure of PDB 2y0e Chain A

Receptor sequence
>2y0eA (length=461) Species: 292 (Burkholderia cepacia) [Search protein sequence]
GSMNLTIIGSGYVGLVTGACLADIGHDVFCLDVDQAKIDILNNGGVPIHE
PGLKEVIARNRSAGRLRFSTDIEAAVAHGDVQFIAVGTPPDEDGSADLQY
VLAAARNIGRYMTGFKVIVDKSTVPVGTAERVRAAVAEELAKRGGDQMFS
VVSNPEFLKEGAAVDDFTRPDRIVIGCDDDVPGERARELMKKLYAPFNRN
HERTLYMDVRSAEFTKYAANAMLATRISFMNELANLADRFGADIEAVRRG
IGSDPRIGYHFLYAGCGYGGSCFPKDVEALIRTADEHGQSLQILKAVSSV
NATQKRVLADKIVARFGEDLTGRTFAIWGLAFKPNTDDMREAPSRELIAE
LLSRGARIAAYDPVAQEEARRVIALDLADHPSWLERLSFVDDEAQAARDA
DALVIVTEWKIFKSPDFVALGRLWKTPVIFDGRNLYEPETMSEQGIEYHP
IGRPGSRQAVA
3D structure
PDB2y0e Structure of Burkholderia Cepacia Udp-Glucose Dehydrogenase (Ugd) Bcec and Role of Tyr10 in Final Hydrolysis of Ugd Thioester Intermediate.
ChainA
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) T123 E160 K216 N220 C272 D276
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 A Y10 E154 F155 L156 K214 I225 F259 Y261 Y266 C270 F271 F330 K331 Y12 E156 F157 L158 K216 I227 F261 Y263 Y268 C272 F273 F332 K333
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:2y0e, PDBe:2y0e, PDBj:2y0e
PDBsum2y0e
PubMed21602353
UniProtC9E261

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