Structure of PDB 3u6w Chain B Binding Site BS02

Receptor Information
>3u6w Chain B (length=405) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRV
IDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSA
SQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAPRAIVH
FYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSP
ESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSI
EWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGE
RTGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNQLPVHERHPYG
GDLVYTAFSGSHQDAINKGLDAMKLDADCDVDDMLWQVPYLPIDPRDVGR
TYEAV
Ligand information
Ligand IDKIV
InChIInChI=1S/C5H8O3/c1-3(2)4(6)5(7)8/h3H,1-2H3,(H,7,8)
InChIKeyQHKABHOOEWYVLI-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(C(=O)O)C(C)C
CACTVS 3.341CC(C)C(=O)C(O)=O
OpenEye OEToolkits 1.5.0CC(C)C(=O)C(=O)O
FormulaC5 H8 O3
Name3-METHYL-2-OXOBUTANOIC ACID;
ALPHA-KETOISOVALERIC ACID;
KETOVALINE
ChEMBLCHEMBL146554
DrugBankDB04074
ZINCZINC000001532553
PDB chain3u6w Chain B Residue 427 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3u6w Removal of the C-terminal regulatory domain of alpha-isopropylmalate synthase disrupts functional substrate binding.
Resolution2.21 Å
Binding residue
(original residue number in PDB)		R80 L143 E218 P252 T254 H285 H287
Binding residue
(residue number reindexed from 1)		R63 L126 E201 P235 T237 H268 H270
Annotation score5
Binding affinityMOAD: Kd=120nM
PDBbind-CN: -logKd/Ki=6.92,Kd=120nM
Enzymatic activity
Enzyme Commision number 2.3.3.13: 2-isopropylmalate synthase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003852 2-isopropylmalate synthase activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0009098 L-leucine biosynthetic process
GO:0019752 carboxylic acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3u6w, PDBe:3u6w, PDBj:3u6w
PDBsum3u6w
PubMed22352945
UniProtP9WQB3|LEU1_MYCTU 2-isopropylmalate synthase (Gene Name=leuA)

[Back to BioLiP]