Structure of PDB 5kah Chain H

Receptor sequence
>5kahH (length=418) Species: 55952 (Streptomyces toyocaensis) [Search protein sequence]
TDGLWAALTEAAASVEKLLATLPEHGARSSAERAEIAAAHDAARALRVRF
LDTHADAVYDRLTDHRRVHLRLAELVEAAATAFPGLVPTQQQLAVERSLP
QAAKEGHEIDQGIFLRAVLRSPLAGPHLLDAMLRPTPRALELLPEFVRTG
EVEMEAVHLERRDGVARLTMCRDDRLNAEDGQQVDDMETAVDLALLDPGV
RVGLLRGGVMSHPRYRGKRVFSAGINLKYLSQGGISLVDFLMRRELGYIH
KLVRGVLTNDDRPGWWHSPRIEKPWVAAVDGFAIGGGAQLLLVFDRVLAS
SDAYFSLPGIIPGAANLRLGRFAGPRVSRQVILEGRRIWAKEPEARLLVD
EVVEPDELDAAIERSLTRLDGDAVLANRRMLNLADESPDGFRAYMAEFAL
MQALRLYGHDTIDKVGRF
3D structure
PDB5kah Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase.
ChainH
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) I225 G286 Q289
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 H L186 A188 E189 H222 Y225 A233 G234 I235 N236 L237 K238 R254 I294 G296 Q299 I325 G327 F432 L176 A178 E179 H212 Y215 A223 G224 I225 N226 L227 K228 R244 I284 G286 Q289 I311 G313 F418
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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