Structure of PDB 2y42 Chain D

Receptor sequence
>2y42D (length=355) Species: 274 (Thermus thermophilus) [Search protein sequence]
SMKVAVLPGDGIGPEVTEAALKVLRALDEAEGLGLAYEVFPFGGAAIDAF
GEPFPEPTRKGVEEAEAVLLGSVGGPKWDGLPRKIRPETGLLSLRKSQDL
FANLRPAKVFPGLERLSPLKEEIARGVDVLIVRELTGGIYFGEPRGMSEA
EAWNTERYSKPEVERVARVAFEAARKRRKHVVSVDKANVLEVGEFWRKTV
EEVGRGYPDVALEHQYVDAMAMHLVRSPARFDVVVTGNIFGDILSDLASV
LPGSLGLLPSASLGRGTPVFEPVHGSAPDIAGKGIANPTAAILSAAMMLE
HAFGLVELARKVEDAVAKALLETPPPDLGGSAGTEAFTATVLRHLAAAAL
EHHHH
3D structure
PDB2y42 Atomic Level Description of the Domain Closure in a Dimeric Enzyme: Thermus Thermophilus 3-Isopropylmalate Dehydrogenase.
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y139 K185 D217 D241 D245
Catalytic site (residue number reindexed from 1) Y140 K186 D218 D242 D246
Enzyme Commision number 1.1.1.85: 3-isopropylmalate dehydrogenase.
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 NAD D I11 D78 H273 G274 A276 D278 I279 N286 I12 D79 H274 G275 A277 D279 I280 N287
BS02 MN D D241 D245 D242 D246
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003862 3-isopropylmalate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051287 NAD binding
Biological Process
GO:0009098 L-leucine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2y42, PDBe:2y42, PDBj:2y42
PDBsum2y42
PubMed21387033
UniProtQ5SIY4|LEU3_THET8 3-isopropylmalate dehydrogenase (Gene Name=leuB)

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