Structure of PDB 4g2r Chain B Binding Site BS04

Receptor Information
>4g2r Chain B (length=441) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DPRDPLLRLSNFFDDGSVELLHERDRSGVLAAAGTVNGVRTIAFCTDGTV
MGGAMGVEGCTHIVNAYDTAIEDQSPIVGIWHSGGARLAEGVRALHAVGQ
VFEAMIRASGYIPQISVVVGFAAGGAAYGPALTDVVVMAPESRVFVTGPM
ASLGGPETHHKKSGVCHIVADDELDAYDRGRRLVGLFCQQGHFDRSKAEA
GDTDIHALLPESSRRAYDVRPIVTAILDADTPFDEFQANWAPSMVVGLGR
LSGRTVGVLANNPLRLGGCLNSESAEKAARFVRLCDAFGIPLVVVVDVPG
YLPGVDQEWGGVVRRGAKLLHAFGECTVPRVTLVTRKTYGGAYIAMNSRS
LNATKVFAWPDAEVAVMGAKAAVGILHKKKLAAAPEHEREALHDQLAAEH
ERIAGGVDSALDIGVVDEKIDPAHTRSKLTEALAQAPARRG
Ligand information
Ligand IDH1L
InChIInChI=1S/C15H11ClF3NO4/c1-8(14(21)22)23-10-2-4-11(5-3-10)24-13-12(16)6-9(7-20-13)15(17,18)19/h2-8H,1H3,(H,21,22)/t8-/m1/s1
InChIKeyGOCUAJYOYBLQRH-MRVPVSSYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)C(Oc2ccc(Oc1ncc(cc1Cl)C(F)(F)F)cc2)C
CACTVS 3.370C[C@@H](Oc1ccc(Oc2ncc(cc2Cl)C(F)(F)F)cc1)C(O)=O
OpenEye OEToolkits 1.7.6CC(C(=O)O)Oc1ccc(cc1)Oc2c(cc(cn2)C(F)(F)F)Cl
OpenEye OEToolkits 1.7.6C[C@H](C(=O)O)Oc1ccc(cc1)Oc2c(cc(cn2)C(F)(F)F)Cl
CACTVS 3.370C[CH](Oc1ccc(Oc2ncc(cc2Cl)C(F)(F)F)cc1)C(O)=O
FormulaC15 H11 Cl F3 N O4
Name(2R)-2-(4-{[3-chloro-5-(trifluoromethyl)pyridin-2-yl]oxy}phenoxy)propanoic acid;
HALOXYFOP INHIBITOR, R enantiomer
ChEMBLCHEMBL1233202
DrugBankDB07870
ZINCZINC000000902175
PDB chain4g2r Chain B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4g2r Structure, Activity, and Inhibition of the Carboxyltransferase beta-Subunit of Acetyl Coenzyme A Carboxylase (AccD6) from Mycobacterium tuberculosis.
Resolution2.28 Å
Binding residue
(original residue number in PDB)		A140 V159 H184 H185 S188 V190
Binding residue
(residue number reindexed from 1)		A127 V146 H159 H160 S163 V165
Annotation score1
Binding affinityMOAD: Kd=35.8uM
PDBbind-CN: -logKd/Ki=4.45,Kd=35.8uM
Enzymatic activity
Catalytic site (original residue number in PDB) A99 G137 G138 Y326 G366 A367
Catalytic site (residue number reindexed from 1) A86 G124 G125 Y301 G341 A342
Enzyme Commision number 2.1.3.-
2.1.3.15: acetyl-CoA carboxytransferase.
Gene Ontology
Molecular Function
GO:0003989 acetyl-CoA carboxylase activity
GO:0004658 propionyl-CoA carboxylase activity
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0016874 ligase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0019367 fatty acid elongation, saturated fatty acid
Cellular Component
GO:0009274 peptidoglycan-based cell wall
GO:0009317 acetyl-CoA carboxylase complex

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4g2r, PDBe:4g2r, PDBj:4g2r
PDBsum4g2r
PubMed25092705
UniProtP9WQH5|ACCD6_MYCTU Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta6 subunit (Gene Name=accD6)

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