Structure of PDB 4qdc Chain A Binding Site BS02

Receptor Information
>4qdc Chain A (length=369) Species: 1829 (Rhodococcus rhodochrous) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EIREIQAAAAPTRFARGWHCLGLLRDFQDGKPHSIEAFGTKLVVFADSKG
QLNVLDAYCRHMGGDLSRGEVKGDSIACPFHDWRWNGKGKCTDIPYARRV
PPIAKTRAWTTLERNGQLYVWNDPQGNPPPEDVTIPEIAGYGTDEWTDWS
WKSLRIKGSHCREIVDNVVDMAHFFYIHYSFPRYFKNVFEGHTATQYMHS
TGREDVISGTNYDDPNAELRSEATYFGPSYMIDWLESDANGQTIETILIN
CHYPVSNNEFVLQYGAIVKKLPGVSDEIAAGMAEQFAEGVQLGFEQDVEI
WKNKAPIDNPLLSEEDGPVYQLRRWYQQFYVDVEDITEDMTKRFEFEIDT
TRAVASWQKEVAENLAKQA
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain4qdc Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4qdc Substrate specificities and conformational flexibility of 3-ketosteroid 9 alpha-hydroxylases.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		N181 H187 H192 D311
Binding residue
(residue number reindexed from 1)		N167 H173 H178 D297
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.15.30: 3-ketosteroid 9alpha-monooxygenase.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4qdc, PDBe:4qdc, PDBj:4qdc
PDBsum4qdc
PubMed25049233
UniProtF1CMY8|KSHA5_RHORH 3-ketosteroid-9-alpha-monooxygenase, oxygenase component (Gene Name=kshA)

[Back to BioLiP]