Structure of PDB 3hq1 Chain A

Receptor sequence
>3hq1A (length=573) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRV
IDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSA
SQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAPRAIVH
FYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSP
ESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSI
EWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGE
RTGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNQLPVHERHPYG
GDLVYTAFSGSHQDAINKGLDAMKLDADAADCDVDDMLWQVPYLPIDPRD
VGRTYEAVIKGGVAYIMKTDHGLSLPRRLQIEFSQVIQKIEVSPKEMWDA
FAEEYLAPVRPLERIRQHVDAADDDGGTTSITATVKINGVETEISGSGNG
PLAAFVHALADVGFDVAVLDYYEHAMSAGDDAQAAAYVEASVTISKTVWG
VGIAPSITTASLRAVVSAVNRAA
3D structure
PDB3hq1 Probing the active site of M. tuberculosis LeuA
ChainA
Resolution1.7 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 A D81 H285 H287 N321 D64 H268 H270 N304
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003852 2-isopropylmalate synthase activity
GO:0003985 acetyl-CoA C-acetyltransferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0030145 manganese ion binding
GO:0030955 potassium ion binding
GO:0046872 metal ion binding
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
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3hq1, PDBe:3hq1, PDBj:3hq1
PDBsum3hq1
PubMed
UniProtP9WQB3|LEU1_MYCTU 2-isopropylmalate synthase (Gene Name=leuA)

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