Structure of PDB 5kah Chain C

Receptor sequence
>5kahC (length=417) Species: 55952 (Streptomyces toyocaensis) [Search protein sequence]
DGLWAALTEAAASVEKLLATLPEHGARSSAERAEIAAAHDAARALRVRFL
DTHADAVYDRLTDHRRVHLRLAELVEAAATAFPGLVPTQQQLAVERSLPQ
AAKEGHEIDQGIFLRAVLRSPLAGPHLLDAMLRPTPRALELLPEFVRTGE
VEMEAVHLERRDGVARLTMCRDDRLNAEDGQQVDDMETAVDLALLDPGVR
VGLLRGGVMSHPRYRGKRVFSAGINLKYLSQGGISLVDFLMRRELGYIHK
LVRGVLTNDDRPGWWHSPRIEKPWVAAVDGFAIGGGAQLLLVFDRVLASS
DAYFSLPGIIPGAANLRLGRFAGPRVSRQVILEGRRIWAKEPEARLLVDE
VVEPDELDAAIERSLTRLDGDAVLANRRMLNLADESPDGFRAYMAEFALM
QALRLYGHDTIDKVGRF
3D structure
PDB5kah Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase.
ChainC
Resolution2.779 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
Catalytic site (residue number reindexed from 1) I224 G285 Q288
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 C R185 L186 A188 E189 H222 R224 Y225 A233 G234 I235 N236 L237 K238 F250 R254 F292 I324 I325 G327 F432 R174 L175 A177 E178 H211 R213 Y214 A222 G223 I224 N225 L226 K227 F239 R243 F281 I309 I310 G312 F417
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:5kah, PDBe:5kah, PDBj:5kah
PDBsum5kah
PubMed28695857
UniProtQ8KLK7|DPGC_STRTO (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase (Gene Name=BU52_01220)

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