Structure of PDB 2pg8 Chain A

Receptor sequence
>2pg8A (length=417) Species: 55952 (Streptomyces toyocaensis) [Search protein sequence]
DTDGLWAALTEAAASVEKLLATLPEHGARSSAERAEIAAAHDAARALRVR
FLDTHADAVYDRLTDHRRVHLRLAELVEAAATAFPGLVPTQQQLAVERSL
PQAAKEGHEIDQGIFLRAVLRSPLAGPHLLDAMLRPTPRALELLPEFVRT
GEVEMEAVHLERRDGVARLTMCRDDRLNAEDGQQVDDMETAVDLALLDPG
VRVGLLRGGVMSHPRYRGKRVFSAGINLKYLSQGGISLVDFLMRKELGYI
HKLVRGVLTNDDRPGWWHSPRIEKPWVAAVDGFAIGGGAQLLLVFDRVLA
SSDAYFSLPAAKEGIIPGAANLRLGRFAGPRVSRQVILEGRRIWAKEPEA
RLLVDEVVEPDELDAAIERSLTRLDGDAVLANRRMLNLADESPDGFRAYM
AEFALMQALRLYGHDVI
3D structure
PDB2pg8 Substrate Recognition and Catalysis by the Cofactor-Independent Dioxygenase DpgC.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I235 G296 Q299 A319
Catalytic site (residue number reindexed from 1) I226 G287 Q290 A310
Enzyme Commision number 1.13.11.80: (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase.
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 YE1 A R185 L186 E189 H222 Y225 A233 G234 I235 N236 L251 K254 G295 G296 Q299 G327 R176 L177 E180 H213 Y216 A224 G225 I226 N227 L242 K245 G286 G287 Q290 G318
BS02 OXY A A319 I324 A310 I315
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0042802 identical protein binding
Biological Process
GO:0006635 fatty acid beta-oxidation
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2pg8, PDBe:2pg8, PDBj:2pg8
PDBsum2pg8
PubMed18004875
UniProtQ8KLK7|DPGC_STRTO (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase (Gene Name=BU52_01220)

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