Structure of PDB 4qdd Chain A

Receptor sequence
>4qddA (length=366) Species: 1829 (Rhodococcus rhodochrous) [Search protein sequence]
EIREIQAAAAPTRFARGWHCLGLLRDFQDGKPHSIEAFGTKLVVFADSKG
QLNVLDAYCRHMGGDLSRGEVKGDSIACPFHDWRWNGKGKCTDIPYARRV
PPIAKTRAWTTLERNGQLYVWNDPQGNPPPEDVTIPEIAGYGTDEWTDWS
WKSLRIKGSHCREIVDNVVDMAHFFYIHYSFPRYFKNVFEGHTATQYMHS
TGREDVISYDDPNAELRSEATYFGPSYMIDWLESDANGQTIETILINCHY
PVSNNEFVLQYGAIVKKLPGVSDEIAAGMAEQFAEGVQLGFEQDVEIWKN
KAPIDNPLLSEEDGPVYQLRRWYQQFYVDVEDITEDMTKRFEFEIDTTRA
VASWQKEVAENLAKQA
3D structure
PDB4qdd Substrate specificities and conformational flexibility of 3-ketosteroid 9 alpha-hydroxylases.
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.15.30: 3-ketosteroid 9alpha-monooxygenase.
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 FES A C73 H75 M76 G78 C92 F94 H95 W97 C59 H61 M62 G64 C78 F80 H81 W83
BS02 FE2 A H187 H192 D311 H173 H178 D294
BS03 30Q A N181 V182 H192 Q210 D247 F300 G303 N167 V168 H178 Q196 D230 F283 G286
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0036200 3-ketosteroid 9-alpha-monooxygenase activity
GO:0046872 metal ion binding
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0006707 cholesterol catabolic process
GO:0008203 cholesterol metabolic process
GO:0016042 lipid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4qdd, PDBe:4qdd, PDBj:4qdd
PDBsum4qdd
PubMed25049233
UniProtF1CMY8|KSHA5_RHORH 3-ketosteroid-9-alpha-monooxygenase, oxygenase component (Gene Name=kshA)

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