Structure of PDB 1cnz Chain A

Receptor sequence
>1cnzA (length=363) [Search protein sequence]
MSKNYHIAVLPGDGIGPEVMAQALKVMDAVRSRFDMRITTSHYDVGGIAI
DNHGHPLPKATVEGCEQADAILFGSVGGPKWENLPPESQPERGALLPLRK
HFKLFSNLRPAKLYQGLEAFCPLRADIAANGFDILCVRELTGGIYFGQPK
GREGSGQYEKAFDTEVYHRFEIERIARIAFESARKRRRKVTSIDKANVLQ
SSILWREIVNDVAKTYPDVELAHMYIDNATMQLIKDPSQFDVLLCSNLFG
DILSDECAMITGSMGMLPSASLNEQGFGLYEPAGGSAPDIAGKNIANPIA
QILSLALLLRYSLDANDAATAIEQAINRALEEGVRTGDLARGAAAVSTDE
MGDIIARYVAEGV
3D structure
PDB1cnz Crystal Structures of Eschericia Coli and Salmonella Typhimurium 3- Isopropylmalate Dehydrogenase and Comparison with Their Thermophilic Counterpart from Thermus Thermophilus
ChainA
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y145 K195 D227 D251
Catalytic site (residue number reindexed from 1) Y145 K195 D227 D251
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 MN A D251 D255 D251 D255
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1cnz, PDBe:1cnz, PDBj:1cnz
PDBsum1cnz
PubMed9086278
UniProtP37412|LEU3_SALTY 3-isopropylmalate dehydrogenase (Gene Name=leuB)

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