Structure of PDB 4f7i Chain D

Receptor sequence
>4f7iD (length=349) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
SMKVAVLPGDGIGPEVTEAALKVLRALDEAEGLGLAYEVFPFGGAAIDAF
GEPFPEPTRKGVEEAEAVLLGSVGGPKWDGLPRKIRPETGLLSLRKSQDL
FANLRPAKVFPGLERLSPLKEEIARGVDVLIVRELTGGIYFGEPRGMSEA
EAWNTERYSKPEVERVARVAFEAARKRRKHVVSVDKANVLEVGEFWRKTV
EEVGRGYPDVALEHQYVDAMAMHLVRSPARFDVVVTGNIFGDILSDLASV
LPGSLGLLPSASLGRGTPVFEPVHGSAPDIAGKGIANPTAAILSAAMMLE
HAFGLVELARKVEDAVAKALLETPPPDLGGSAGTEAFTATVLRHLAAAA
3D structure
PDB4f7i Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis.
ChainD
Resolution2.0 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 N187 Y215 N188 Y216
BS02 IPM D R94 R104 R132 Y139 D241 R95 R105 R133 Y140 D242
BS03 NAD D I11 S71 V72 G73 E87 G255 H273 G274 S275 A276 D278 I279 N286 I12 S72 V73 G74 E88 G256 H274 G275 S276 A277 D279 I280 N287
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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Cellular Component
External links
PDB RCSB:4f7i, PDBe:4f7i, PDBj:4f7i
PDBsum4f7i
PubMed25211160
UniProtQ5SIY4|LEU3_THET8 3-isopropylmalate dehydrogenase (Gene Name=leuB)

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