Structure of PDB 2xc3 Chain A Binding Site BS02

Receptor Information
>2xc3 Chain A (length=409) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SPNLPPGFDFTDPAIYAERLPVAEFAELRSAAPIWWNGQDPGKGGGFHDG
GFWAITKLNDVKEISRHSDVFSSYENGVIPRFKNDIAREDIEVQRFVMLN
MDAPHHTRLRKIISRGFTPRAVGRLHDELQERAQKIAAEAAAAGSGDFVE
QVSCELPLQAIAGLLGVPQEDRGKLFHWSNEMTGNEDPEYAHIDPKASSA
ELIGYAMKMAEEKADIVTQLIQADIDGEKLSDDEFGFFVVMLAVAGNETT
RNSITQGMMAFAEHPDQWELYKKVRPETAADEIVRWATPVTAFQRTALRD
YELSGVQIKKGQRVVMFYRSANFDEEVFQDPFTFNILRNPNPHVGFGGTG
AHYCIGANLARMTINLIFNAVADHMPDLKPISAPERLRSGWLNGIKHWQV
DYTGRLPVA
Ligand information
Ligand IDRT8
InChIInChI=1S/C24H28N4O2/c1-16-6-8-17(9-7-16)23(29)28-22(24(30)27-19-10-12-25-13-11-19)14-18-15-26-21-5-3-2-4-20(18)21/h2-5,10-13,15-17,22,26H,6-9,14H2,1H3,(H,28,29)(H,25,27,30)/t16-,17-,22-/m1/s1
InChIKeyICFUCABJWQGTGU-DRSNIGMVSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(Nc1ccncc1)C(NC(=O)C2CCC(C)CC2)Cc4c3ccccc3nc4
OpenEye OEToolkits 1.6.1CC1CCC(CC1)C(=O)NC(Cc2c[nH]c3c2cccc3)C(=O)Nc4ccncc4
CACTVS 3.352C[CH]1CC[CH](CC1)C(=O)N[CH](Cc2c[nH]c3ccccc23)C(=O)Nc4ccncc4
OpenEye OEToolkits 1.6.1CC1CCC(CC1)C(=O)N[C@H](Cc2c[nH]c3c2cccc3)C(=O)Nc4ccncc4
CACTVS 3.352C[C@@H]1CC[C@H](CC1)C(=O)N[C@H](Cc2c[nH]c3ccccc23)C(=O)Nc4ccncc4
FormulaC24 H28 N4 O2
NameNALPHA-[(TRANS-4-METHYLCYCLOHEXYL)CARBONYL]-N-PYRIDIN-4-YL-D-TRYPTOPHANAMIDE
ChEMBL
DrugBank
ZINC
PDB chain2xc3 Chain A Residue 1434 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2xc3 Reverse Type I Inhibitor of Mycobacteriumtuberculosis Cyp125A1.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		I97 F100 D108 Q112 L117 T201 V263 V267 W414
Binding residue
(residue number reindexed from 1)		I79 F82 D90 Q94 L99 T183 V240 V244 W391
Annotation score1
Binding affinityMOAD: Kd=1.68uM
Enzymatic activity
Catalytic site (original residue number in PDB) G202 A268 E271 T272 T273 C377 I378 G379 T386 L415
Catalytic site (residue number reindexed from 1) G184 A245 E248 T249 T250 C354 I355 G356 T363 L392
Enzyme Commision number 1.14.15.29: cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming].
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0036199 cholest-4-en-3-one 26-monooxygenase activity
GO:0046872 metal ion binding
Biological Process
GO:0006707 cholesterol catabolic process
GO:0008203 cholesterol metabolic process
GO:0016042 lipid catabolic process
GO:0051701 biological process involved in interaction with host

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2xc3, PDBe:2xc3, PDBj:2xc3
PDBsum2xc3
PubMed21109436
UniProtP9WPP1|CP125_MYCTU Steroid C26-monooxygenase (Gene Name=cyp125)

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