Structure of PDB 3u6w Chain B

Receptor sequence
>3u6wB (length=405) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRV
IDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSA
SQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAPRAIVH
FYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSP
ESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSI
EWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGE
RTGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNQLPVHERHPYG
GDLVYTAFSGSHQDAINKGLDAMKLDADCDVDDMLWQVPYLPIDPRDVGR
TYEAV
3D structure
PDB3u6w Removal of the C-terminal regulatory domain of alpha-isopropylmalate synthase disrupts functional substrate binding.
ChainB
Resolution2.21 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.3.13: 2-isopropylmalate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN B D81 H285 H287 D64 H268 H270
BS02 KIV B R80 L143 E218 P252 T254 H285 H287 R63 L126 E201 P235 T237 H268 H270 MOAD: Kd=120nM
PDBbind-CN: -logKd/Ki=6.92,Kd=120nM
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

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

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