Structure of PDB 5kaj Chain E

Receptor sequence
>5kajE (length=417) Species: 55952 (Streptomyces toyocaensis) [Search protein sequence]
TDGLWAALTEAAASVEKLLATLPEHGARSSAERAEIAAAHDAARALRVRF
LDTHADAVYDRLTDHRRVHLRLAELVEAAATAFPGLVPTQQQLAVERSLP
QAAKEGHEIDQGIFLRAVLRSPLAGPHLLDAMLRPTPRALELLPEFVRTG
EVEMEAVHLERRDGVARLTMCRDDRLNAEDGQQVDDMETAVDLALLDPGV
RVGLLRGGVMSHPRYRGKRVFSAGINLKYLSQGGISLVDFLMRRELGYIH
KLVRGVLTNDDRPGWWHSPRIEKPWVAAVDGFAIGGGAQLLLVFDRVLAS
SDAYFSLPCAKEGIIPGAANLRLGRFAGPRVSRQVILEGRRIWAKEPEAR
LLVDEVVEPDELDAAIERSLTRLDGDAVLANRRMLNLADESPDGFRAYMA
EFALMQALRLYGHDVID
3D structure
PDB5kaj Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase.
ChainE
Resolution2.681 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 C319
Catalytic site (residue number reindexed from 1) I225 G286 Q289 C309
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 YE2 E L186 E189 H222 R224 Y225 A233 G234 I235 N236 L237 K238 F250 L251 R254 I294 G295 G296 Q299 P318 C319 E322 I325 G327 L176 E179 H212 R214 Y215 A223 G224 I225 N226 L227 K228 F240 L241 R244 I284 G285 G286 Q289 P308 C309 E312 I315 G317
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:5kaj, PDBe:5kaj, PDBj:5kaj
PDBsum5kaj
PubMed28695857
UniProtQ8KLK7|DPGC_STRTO (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase (Gene Name=BU52_01220)

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