Structure of PDB 5kah Chain L

Receptor sequence
>5kahL (length=418) Species: 55952 (Streptomyces toyocaensis) [Search protein sequence]
GLWAALTEAAASVEKLLATLPEHGARSSAERAEIAAAHDAARALRVRFLD
THADAVYDRLTDHRRVHLRLAELVEAAATAFPGLVPTQQQLAVERSLPQA
AKEGHEIDQGIFLRAVLRSPLAGPHLLDAMLRPTPRALELLPEFVRTGEV
EMEAVHLERRDGVARLTMCRDDRLNAEDGQQVDDMETAVDLALLDPGVRV
GLLRGGVMSHPRYRGKRVFSAGINLKYLSQGGISLVDFLMRRELGYIHKL
VRGVLTNDDRPGWWHSPRIEKPWVAAVDGFAIGGGAQLLLVFDRVLASSD
AYFSLPAAGIIPGAANLRLGRFAGPRVSRQVILEGRRIWAKEPEARLLVD
EVVEPDELDAAIERSLTRLDGDAVLANRRMLNLADESPDGFRAYMAEFAL
MQALRLYGHDTIDKVGRF
3D structure
PDB5kah Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase.
ChainL
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 A319
Catalytic site (residue number reindexed from 1) I223 G284 Q287 A307
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 L E189 H222 R224 Y225 A233 G234 I235 N236 L237 K238 R254 G296 Q299 P318 I324 I325 G327 F432 E177 H210 R212 Y213 A221 G222 I223 N224 L225 K226 R242 G284 Q287 P306 I310 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

View graph for
Molecular Function

View graph for
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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