Structure of PDB 2x5l Chain A Binding Site BS01

Receptor Information
>2x5l Chain A (length=414) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PNLPPGFDFTDPAIYAERLPVAEFAELRSAAPIWWNGQDPGKGGGFHDGG
FWAITKLNDVKEISRHSDVFSSYENGVIPRFKNDIAREDIEVQRFVMLNM
DAPHHTRLRKIISRGFTPRAVGRLHDELQERAQKIAAEAAAAGSGDFVEQ
VSCELPLQAIAGLLGVPQEDRGKLFHWSNEMTGNEDPEYAHIDPKASSAE
LIGYAMKMAEEKAKNPADDIVTQLIQADIDGEKLSDDEFGFFVVMLAVAG
NETTRNSITQGMMAFAEHPDQWELYKKVRPETAADEIVRWATPVTAFQRT
ALRDYELSGVQIKKGQRVVMFYRSANFDEEVFQDPFTFNILRNPNPHVGF
GGTGAHYCIGANLARMTINLIFNAVADHMPDLKPISAPERLRSGWLNGIK
HWQVDYTGRLPVAH
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain2x5l 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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PDB2x5l Reverse Type I Inhibitor of Mycobacteriumtuberculosis Cyp125A1.
Resolution1.48 Å
Binding residue
(original residue number in PDB)		M116 L117 H124 R128 M264 A268 G269 T272 T273 P312 F316 R318 G368 F369 G370 H375 C377 I378 G379 A383
Binding residue
(residue number reindexed from 1)		M97 L98 H105 R109 M245 A249 G250 T253 T254 P293 F297 R299 G349 F350 G351 H356 C358 I359 G360 A364
Annotation score1
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) G183 A249 E252 T253 T254 C358 I359 G360 T367 L396
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:2x5l, PDBe:2x5l, PDBj:2x5l
PDBsum2x5l
PubMed21109436
UniProtP9WPP1|CP125_MYCTU Steroid C26-monooxygenase (Gene Name=cyp125)

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