Structure of PDB 2zyl Chain A

Receptor sequence
>2zylA (length=359) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
DAGALPTRYARGWHCLGVAKDYLEGKPHGVEAFGTKLVVFADSHGDLKVL
DGYCRHMGGDLSEGTVKGDEVACPFHDWRWGGDGRCKLVPYARRTPRMAR
TRSWTTDVRSGLLFVWHDHEGNPPDPAVRIPEIPEAASDEWTDWRWNRIL
IEGSNCRDIIDNVTDMAHFFYIHFGLPTYFKNVFEGHIASQYLHNVGRPD
VDDLGTSYGEAHLDSEASYFGPSFMINWLHNRYGNYKSESILINCHYPVT
QNSFVLQWGVIVEKPKGMSMTDKLSRVFTEGVSKGFLQDVEIWKHKTRID
NPLLVEEDGAVYQLRRWYEQFYVDVADIKPEMVERFEIEVDTKRANEFWN
AEVEKNLKS
3D structure
PDB2zyl Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis
ChainA
Resolution2.3 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 C67 H69 M70 C86 F88 H89 W91 C54 H56 M57 C73 F75 H76 W78
BS02 FE2 A H181 H186 D304 H168 H173 D289
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:0047086 ketosteroid monooxygenase activity
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0006694 steroid biosynthetic process
GO:0006707 cholesterol catabolic process
GO:0008203 cholesterol metabolic process
GO:0016042 lipid catabolic process
GO:0070207 protein homotrimerization
GO:0070723 response to cholesterol
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2zyl, PDBe:2zyl, PDBj:2zyl
PDBsum2zyl
PubMed19234303
UniProtP71875|KSHA_MYCTU 3-ketosteroid-9-alpha-monooxygenase, oxygenase component (Gene Name=kshA)

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