Structure of PDB 1a05 Chain A

Receptor sequence

>1a05A (length=357) Species: 920 (Acidithiobacillus ferrooxidans)

MKKIAIFAGDGIGPEIVAAARQVLDAVDQAAHLGLRCTEGLVGGAALDAS
DDPLPAASLQLAMAADAVILGAVGGPRWDAYPPAKRPEQGLLRLRKGLDL
YANLRPAQIFPQLLDASPLRPELVRDVDILVVRELTGDIYFGQPRGLEVI
DGKRRGFNTMVYDEDEIRRIAHVAFRAAQGRRKQLCSVDKANVLETTRLW
REVVTEVARDYPDVRLSHMYVDNAAMQLIRAPAQFDVLLTGNMFGDILSD
EASQLTGSIGMLPSASLGEGRAMYEPIHGSAPDIAGQDKANPLATILSVA
MMLRHSLNAEPWAQRVEAAVQRVLDQGLRTADIAAPGTPVIGTKAMGAAV
VNALNLK

3D structure

• PDB: 1a05 Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y140 K190 D222 D246 D250
• Catalytic site (residue number reindexed from 1): Y140 K190 D222 D246 D250
• 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	IPM	A	R95 R105 R133 Y140 D246	R95 R105 R133 Y140 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:0046872 metal ion binding
• GO:0051287 NAD binding

Biological Process

• GO:0009098 L-leucine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1a05, PDBe:1a05, PDBj:1a05
• PDBsum: 1a05
• PubMed: 9739088
• UniProt: Q56268|LEU3_ACIFR 3-isopropylmalate dehydrogenase (Gene Name=leuB)