Structure of PDB 2wuf Chain B Binding Site BS01

Receptor Information
>2wuf Chain B (length=282) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LTFESTSRFAEVDVDGPLKLHYHEAGVGNDQTVVLLHGGGPGAASWTNFS
RNIAVLARHFHVLAVDQPGYGHSDKRAEHGQFNRYAAMALKGLFDQLGLG
RVPLVGNALGGGTAVRFALDYPARAGRLVLMGPGGLSINLFAPDPTEGVK
RLSKFSVAPTRENLEAFLRVMVYDKNLITPELVDQRFALASTPESLTATR
AMGKSFAGADFEAGMMWREVYRLRQPVLLIWGREDRVNPLDGALVALKTI
PRAQLHVFGQCGHWVQVEKFDEFNKLTIEFLG
Ligand information
Ligand IDKEM
InChIInChI=1S/C19H26O6/c1-11(3-6-16(22)18(24)25)14(20)7-4-12-13-5-8-17(23)19(13,2)10-9-15(12)21/h3,6,11-13,17,23H,4-5,7-10H2,1-2H3,(H,24,25)/p-1/b6-3+/t11-,12-,13-,17+,19+/m1/s1
InChIKeyPAPYZGVUTPWUFW-WDRCEGBMSA-M
SMILES
SoftwareSMILES
CACTVS 3.352C[C@H](\C=C\C(=O)C([O-])=O)C(=O)CC[C@@H]1[C@H]2CC[C@H](O)[C@@]2(C)CCC1=O
OpenEye OEToolkits 1.6.1C[C@H](\C=C\C(=O)C(=O)[O-])C(=O)CC[C@@H]1[C@H]2CC[C@@H]([C@]2(CCC1=O)C)O
CACTVS 3.352C[CH](C=CC(=O)C([O-])=O)C(=O)CC[CH]1[CH]2CC[CH](O)[C]2(C)CCC1=O
OpenEye OEToolkits 1.6.1CC(C=CC(=O)C(=O)[O-])C(=O)CCC1C2CCC(C2(CCC1=O)C)O
ACDLabs 10.04[O-]C(=O)C(=O)\C=C\C(C(=O)CCC1C(=O)CCC2(C1CCC2O)C)C
FormulaC19 H25 O6
Name(3E,5R)-8-[(1S,3AR,4R,7AS)-1-HYDROXY-7A-METHYL-5-OXOOCTAHYDRO-1H-INDEN-4-YL]-5-METHYL-2,6-DIOXOOCT-3-ENOATE
ChEMBL
DrugBank
ZINC
PDB chain2wuf Chain B Residue 1289 [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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PDB2wuf Characterization of a carbon-carbon hydrolase from Mycobacterium tuberculosis involved in cholesterol metabolism.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G44 G45 G46 A114 L115 L158 F212 H269 W270
Binding residue
(residue number reindexed from 1)		G38 G39 G40 A108 L109 L152 F206 H263 W264
Annotation score1
Binding affinityMOAD: Kd=51uM
PDBbind-CN: -logKd/Ki=4.29,Kd=51uM
Enzymatic activity
Catalytic site (original residue number in PDB) G45 G46 G48 N113 A114 L115 R192 D241 H269 W270
Catalytic site (residue number reindexed from 1) G39 G40 G42 N107 A108 L109 R186 D235 H263 W264
Enzyme Commision number 3.7.1.17: 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase.
3.7.1.8: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0018774 2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity
GO:0102296 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase activity
Biological Process
GO:0006694 steroid biosynthetic process
GO:0016042 lipid catabolic process
GO:0051701 biological process involved in interaction with host
Cellular Component
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2wuf, PDBe:2wuf, PDBj:2wuf
PDBsum2wuf
PubMed19875455
UniProtP9WNH5|HSAD_MYCTU 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase (Gene Name=hsaD)

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